The Pex5p receptor recognizes newly synthesized peroxisomal matrix proteins which have a C-terminal peroxisomal targeting signal to the peroxisome. After docking to protein complexes on the membrane, these proteins are translocated across the membrane. The docking mechanism remains unclear, as no structural data on the multicomponent docking complex are available. As the interaction of the cargo-loaded Pex5p receptor and the peroxisomal membrane protein Pex14p is the essential primary docking step, we have investigated the solution structure of these complexes by small angle x-ray scattering and static light scattering. Titration studies yielded a 1:6 stoichiometry for the Pex5p·Pex14p complex, and low resolution structural models were reconstructed from the x-ray scattering data. The free full-length human Pex5p is monomeric in solution, with an elongated, partially unfolded N-terminal domain. The model of the complex reveals that the N terminus of Pex5p remains extended in the presence of cargo and Pex14p, the latter proteins being significantly intermingled with the Pex5p moiety. These results suggest that the extended structure of Pex5p may play a role in interactions with other substrates such as lipids and membrane proteins during the formation of functional multiprotein complexes. The Pex5p receptor recognizes newly synthesized peroxisomal matrix proteins which have a C-terminal peroxisomal targeting signal to the peroxisome. After docking to protein complexes on the membrane, these proteins are translocated across the membrane. The docking mechanism remains unclear, as no structural data on the multicomponent docking complex are available. As the interaction of the cargo-loaded Pex5p receptor and the peroxisomal membrane protein Pex14p is the essential primary docking step, we have investigated the solution structure of these complexes by small angle x-ray scattering and static light scattering. Titration studies yielded a 1:6 stoichiometry for the Pex5p·Pex14p complex, and low resolution structural models were reconstructed from the x-ray scattering data. The free full-length human Pex5p is monomeric in solution, with an elongated, partially unfolded N-terminal domain. The model of the complex reveals that the N terminus of Pex5p remains extended in the presence of cargo and Pex14p, the latter proteins being significantly intermingled with the Pex5p moiety. These results suggest that the extended structure of Pex5p may play a role in interactions with other substrates such as lipids and membrane proteins during the formation of functional multiprotein complexes. Peroxisomes are ubiquitous organelles in eukaryotes which are involved in different metabolic pathways (1Purdue P.E. Lazarow P.B. Annu. Rev. Cell Dev. Biol. 2001; 17: 701-752Crossref PubMed Scopus (285) Google Scholar). Peroxisomal matrix proteins, which contain a peroxisomal targeting signal (PTS), 4The abbreviations used are:PTSperoxisomal targeting signalsDLSdynamic light scatteringDmaxmaximum particle dimensionEMelectron microscopyMMmolar massNSDnormalized spatial discrepancyp(r)distance distribution functionRgradius of gyrationSAXSsmall angle X-ray scatteringSLSstatic light scatteringSAsimulated annealingTCEPTris(2-carboxyethyl)phosphine hydrochlorideTPRtetratricopeptide repeatNTAnitrilotriacetic acidSCP2sterol carrier protein 2.are imported into the peroxisome by recognition of two different import receptors, Pex5p or Pex7p. These receptors recognize specific signal sequences, PTS1 and PTS2, respectively (1Purdue P.E. Lazarow P.B. Annu. Rev. Cell Dev. Biol. 2001; 17: 701-752Crossref PubMed Scopus (285) Google Scholar). At the molecular level the C-terminal PTS1 signal is bound in a central cavity of the ring-like structure of the seven tetrapeptide repeat (TPR) domains of the C-terminal part of Pex5p (Pex5p(C)) (2Gatto Jr., G.J. Geisbrecht B.V. Gould S.J. Berg J.M. Nat. Struct. Biol. 2000; 7: 1091-1095Crossref PubMed Scopus (300) Google Scholar, 3Kumar A. Roach C. Hirsh I.S. Turley S. deWalque S. Michels P.A. Hol W.G. J. Mol. Biol. 2001; 307: 271-282Crossref PubMed Scopus (43) Google Scholar, 4Stanley W.A. Filipp F.V. Kursula P. Schüller N. Erdmann R. Schliebs W. Sattler M. Wilmanns M. Mol. Cell. 2006; 24: 653-663Abstract Full Text Full Text PDF PubMed Scopus (132) Google Scholar, 5Stanley W.A. Fodor K. Marti-Renom M.A. Schliebs W. Wilmanns M. FEBS Lett. 2007; 581: 4795-4802Crossref PubMed Scopus (21) Google Scholar). It was recently proposed that some of the structural principles of the Pex5p/cargo interaction may also apply to the PTS2 cargo recognition of the Pex7p receptor (5Stanley W.A. Fodor K. Marti-Renom M.A. Schliebs W. Wilmanns M. FEBS Lett. 2007; 581: 4795-4802Crossref PubMed Scopus (21) Google Scholar). peroxisomal targeting signals dynamic light scattering maximum particle dimension electron microscopy molar mass normalized spatial discrepancy distance distribution function radius of gyration small angle X-ray scattering static light scattering simulated annealing Tris(2-carboxyethyl)phosphine hydrochloride tetratricopeptide repeat nitrilotriacetic acid sterol carrier protein 2. The next step of PTS-protein import, docking of the cargo loaded receptor to the translocon, involves the peroxisomal protein Pex14p (6Azevedo J.E. Schliebs W. Biochim. Biophys. Acta. 2006; 1763: 1574-1584Crossref PubMed Scopus (60) Google Scholar). Multiple Pex14p binding sites with di-aromatic pentapeptide motifs (WXXX(F/Y)) were shown to be present in the N terminus of Pex5p (7Nito K. Hayashi M. Nishimura M. Plant. Cell Physiol. 2002; 43: 355-366Crossref PubMed Scopus (84) Google Scholar, 8Saidowsky J. Dodt G. Kirchberg K. Wegner A. Nastainczyk W. Kunau W.H. Schliebs W. J. Biol. Chem. 2001; 276: 34524-34529Abstract Full Text Full Text PDF PubMed Scopus (98) Google Scholar, 9Otera H. Setoguchi K. Hamasaki M. Kumashiro T. Shimizu N. Fujiki Y. Mol. Cell. Biol. 2002; 22: 1639-1655Crossref PubMed Scopus (175) Google Scholar). The number of these motifs, however, varies among species. The human Pex5p receptor, which has been investigated in this contribution, has a total of seven motifs. A recent NMR structure of the N-terminal domain of Pex14p and the first WXXX(F/Y) motif of Pex5p reveals an α-helical conformation of the motif (10Neufeld C. Filipp F.V. Simon B. Neuhaus A. Schüller N. David C. Kooshapur H. Madl T. Erdmann R. Schliebs W. Wilmanns M. Sattler M. EMBO J. 2009; 28: 745-754Crossref PubMed Scopus (68) Google Scholar). Interactions between Pex5p and other proteins and by their association with the peroxisomal membrane possibly lead to dissociation of the PTS-protein from Pex5p (11Gouveia A.M. Guimarães C.P. Oliveira M.E. Sá-Miranda C. Azevedo J.E. J. Biol. Chem. 2003; 278: 4389-4392Abstract Full Text Full Text PDF PubMed Scopus (74) Google Scholar, 12Holroyd C. Erdmann R. FEBS Lett. 2001; 501: 6-10Crossref PubMed Scopus (66) Google Scholar, 13Madrid K.P. De Crescenzo G. Wang S. Jardim A. Mol. Cell. Biol. 2004; 24: 7331-7344Crossref PubMed Scopus (26) Google Scholar). The exact sequence of events in the import mechanism remains, however, unknown. It is in particular unclear how, in contrast with other organelles, peroxisomes can import folded oligomeric, functional proteins (14Schnell D.J. Hebert D.N. Cell. 2003; 112: 491-505Abstract Full Text Full Text PDF PubMed Scopus (191) Google Scholar). Previous biophysical work indicated that the N terminus half of Pex5p is unfolded in vitro (15Carvalho A.F. Costa-Rodrigues J. Correia I. Costa Pessoa J. Faria T.Q. Martins C.L. Fransen M. Sá-Miranda C. Azevedo J.E. J. Mol. Biol. 2006; 356: 864-875Crossref PubMed Scopus (68) Google Scholar, 16Costa-Rodrigues J. Carvalho A.F. Fransen M. Hambruch E. Schliebs W. Sá-Miranda C. Azevedo J.E. J. Biol. Chem. 2005; 280: 24404-24411Abstract Full Text Full Text PDF PubMed Scopus (41) Google Scholar). Recent protease sensitivity assays showed that the proteolytic profiles of the full-length receptor Pex5p(F) change in the presence of PTS1 peptide and the Pex13p Src homology 3 domain, which is another docking factor (16Costa-Rodrigues J. Carvalho A.F. Fransen M. Hambruch E. Schliebs W. Sá-Miranda C. Azevedo J.E. J. Biol. Chem. 2005; 280: 24404-24411Abstract Full Text Full Text PDF PubMed Scopus (41) Google Scholar, 17Gouveia A.M. Reguenga C. Oliveira M.E. Sa-Miranda C. Azevedo J.E. J. Biol. Chem. 2000; 275: 32444-32451Abstract Full Text Full Text PDF PubMed Scopus (100) Google Scholar), indicating conformational changes of Pex5p upon binding these receptor ligands. Furthermore, it was found that Pex5p may even traverse the peroxisomal membrane, leaving only a small N-terminal fragment in the cytosol while exposing the C-terminal TPR domain to the luminal side of the membrane (11Gouveia A.M. Guimarães C.P. Oliveira M.E. Sá-Miranda C. Azevedo J.E. J. Biol. Chem. 2003; 278: 4389-4392Abstract Full Text Full Text PDF PubMed Scopus (74) Google Scholar). Although recognition of many PTS cargos seems to be confined to the C-terminal TPR domains of Pex5p, it has become clear that the N-terminal part of Pex5p is primarily involved in docking of the receptor onto the peroxisomal membrane and other docking factors. Because only poorly diffracting crystals have been purified to date, we investigated its solution structure by small angle x-ray scattering (SAXS) and static light scattering (SLS). Complexes with the PTS1 cargo sterol carrier protein 2 (SCP2), which functions as lipid transfer protein, were also studied as the crystal structure of Pex5p(C)/SCP2 is already known (4Stanley W.A. Filipp F.V. Kursula P. Schüller N. Erdmann R. Schliebs W. Sattler M. Wilmanns M. Mol. Cell. 2006; 24: 653-663Abstract Full Text Full Text PDF PubMed Scopus (132) Google Scholar). Our results indicate that human Pex5p(F) is a monomer with an extended N terminus. The stoichiometry of Pex5p(F)·Pex14p(N)·PTS1 complex has been assessed by titration with SAXS, SLS, and gel filtration, and a low resolution structural model of the complex has been reconstructed in which Pex5p(F) remains extended upon Pex14p(N) binding. Full-length human Pex5p (residues 1–639; Pex5p (F)), the N terminus of human Pex5p (residues 1–335; Pex5p(N)), the C terminus of human Pex5p (residues 268- 602; Pex5p(C)), and the N terminus of Pex14p (residues 16–80 plus tryptophan; Pex14p(N)) were expressed with an N-terminal His6 tag in Escherichia coli BL21(DE3) cells using either the pET9d or pETM11 plasmid vector (EMBL). SCP2 (residues 22–143) (19Stanley W.A. Versluis K. Schultz C. Heck A.J. Wilmanns M. Arch. Biochem. Biophys. 2007; 461: 50-58Crossref PubMed Scopus (8) Google Scholar) was expressed with an N-terminal glutathione S-transferase and His6 tag in E. coli BL21(DE3) cells using the pETM30 plasmid vector (EMBL). E. coli cells, containing and Pex14p(N) in were and by by for E. coli cells, containing a SCP2 were and the by for 3 The was in and with protease protein were Pex5p(F) was purified by a in binding and and a with containing and 2 SCP2 was purified by in binding and in containing and The glutathione S-transferase tag of SCP2 was with protease for 2 The SCP2 from the was and purified in Pex14p(N) was purified by in binding and with containing and were purified by in binding and with the complex, the two of E. coli cells containing and Pex14p(N)) were on for and in with protease The complex was purified by in binding and with containing and 2 The complex was by a of purified Pex5p(F) and SCP2 on for and purified on a with The complex was by a of purified and SCP2 on for and purified on a with the complex, of E. coli cells containing and were on for and in with protease The complex was purified by in binding and in The glutathione S-transferase tag of SCP2 was with protease for 2 The complex from the was and purified in a were and for the using a with a or molar mass The and of proteins were by and dynamic light scattering The of and used in were from their to be and and were of and into a with and with an The the protein by the and the scattering of the The was used to the the J. T. Biochem. PubMed Scopus Google Scholar). A of proteins was used to the The containing the complexes of were on and Pex5p(F) and and were in containing molar of Pex5p(F) and Pex14p(N) between and were on for to complexes and as indicated The containing the complexes of were on a The x-ray scattering data were on the of the on the J. Scopus Google Scholar). of Pex5p and its and complexes with Pex14p(N) and SCP2 proteins were of and the was to to the The data were using a a distance of and a of the of transfer is the scattering was by of with The data were to the of the and the scattering of the was The data were to data were using the J. 2003; Scopus Google Scholar). The scattering and the radius of gyration were using the A. Google Scholar) that small the is as These were also from the scattering using the J. Scopus Google Scholar), which the maximum particle and the distance distribution functions The molecular of the were from the scattering by of The of were as G. X-ray the an was from data to the of the G. X-ray Scholar) for a for the scattering from the proteins the in are to be the in The low resolution of Pex5p(F) and the complex were reconstructed by the Biophys. J. Full Text Full Text PDF PubMed Scopus Google Scholar) and its J. Biol. Chem. 2000; 275: Full Text Full Text PDF PubMed Scopus Google Scholar). These the particle as a of a with is either to the or to the and the latter is by a is either to the or to of the of the complex to (residues 2 for (residues 3 for the first Pex14p(N) protein binding to Pex5p(F) with SCP2 protein, and for other binding Pex14p(N) The particle low resolution by of the and the model is by a of containing the for or for of the of the from a simulated annealing is in and to for a model of or to the is the scattering from a the the scattering are the of in are and and are the from the of the to the and the the transfer the was to scattering from two from complexes of and and two from of and the that has a the were to the resolution of 3 in the of the scattering to 2 The of the to their molecular were used to the the were to the low resolution models of the was using the models of the C-terminal domain of Pex5p (2Gatto Jr., G.J. Geisbrecht B.V. Gould S.J. Berg J.M. Nat. Struct. Biol. 2000; 7: 1091-1095Crossref PubMed Scopus (300) Google Scholar), Pex5p(C)/SCP2 (4Stanley W.A. Filipp F.V. Kursula P. Schüller N. Erdmann R. Schliebs W. Sattler M. Wilmanns M. Mol. Cell. 2006; 24: 653-663Abstract Full Text Full Text PDF PubMed Scopus (132) Google Scholar), and Pex14p(N) as for the and Biophys. J. 2005; Full Text Full Text PDF PubMed Scopus Google Scholar). that the of to of the and from The scattering of the from the complex were from their by the C. J. 28: Scopus Google Scholar). model the structure of Pex5p(F) in solution, the N-terminal was first by of in the Biophys. J. 2005; Full Text Full Text PDF PubMed Scopus Google Scholar) was to a of the N-terminal fragment the scattering from the full-length The results of were to structural using the J. 2003; Scopus Google Scholar) and J. 2001; Scopus Google Scholar). The latter two low or resolution models by of by a normalized spatial discrepancy or in the first the among the between this and in the model is and the is for the in the These are and normalized the between the for the two to indicate that the two models are the model of the of and also the model that the normalized spatial discrepancy with other models in the The low resolution structure of the N-terminal part of Pex5p(F) was used to model the The of SCP2 with to was as in the model of complex in and the of in the latter model was in model was as a in The of Pex14p(N) were and their were by using the Biophys. J. 2005; Full Text Full Text PDF PubMed Scopus Google Scholar). a to an of the scattering data. were for the Pex14p(N) interaction with the WXXX(F/Y) motifs (residues and of on NMR data (10Neufeld C. Filipp F.V. Simon B. Neuhaus A. Schüller N. David C. Kooshapur H. Madl T. Erdmann R. Schliebs W. Wilmanns M. Sattler M. EMBO J. 2009; 28: 745-754Crossref PubMed Scopus (68) Google Scholar) the model of the complex and its conformational were using J. 2001; Scopus Google Scholar). the of other models were and an was The was the with the with to the other The was for the to the Pex5p(F) and and were in containing molar of Pex5p(F) and Pex14p(N) and were for to and their were the of and The and were as The of and were by using The protein were in was for and into a The data were using the A showed no interaction between Pex14p(N) and of and were on a with a using a in the The protein were in The were for and the acid were first to their in human and were studied by gel and by The from in indicate that Pex5p(F) is monomeric and complexes with the used for gel The complex formation was by and and the purified were found to be in the of the in The interaction between Pex5p(F) and Pex14p(N) was assessed by The of as in 2 and 2 to a molar of a molar the that Pex5p(F) or seven in was by a titration of Pex5p from SLS, and complex, 3 complex, 3 complex, 3 3 complex in a and titration on the complex in a The structural of Pex5p(F) from the scattering are in The and particle with from the primary indicating that Pex5p(F) is monomeric in The and are and recent indicating that Pex5p(F) is (15Carvalho A.F. Costa-Rodrigues J. Correia I. Costa Pessoa J. Faria T.Q. Martins C.L. Fransen M. Sá-Miranda C. Azevedo J.E. J. Mol. Biol. 2006; 356: 864-875Crossref PubMed Scopus (68) Google Scholar, 16Costa-Rodrigues J. Carvalho A.F. Fransen M. Hambruch E. Schliebs W. Sá-Miranda C. Azevedo J.E. J. Biol. Chem. 2005; 280: 24404-24411Abstract Full Text Full Text PDF PubMed Scopus (41) Google Scholar). The distance from the data of complexes investigated are in The of the complex is for by X-ray and Google Scholar), to a of the The other functions have profiles of with a maximum that or no complexes with Pex14p(N) and SCP2 are The functions for complexes in the presence of the Pex14p, and that for the cargo complex in the distance between and that this to the between Pex14p in the the conformation of the N terminus of Pex5p(F) is by the of the of different by and the complex, the radius from first data with the radius of gyration from data as for for the full-length Pex5p, significantly an is for unfolded proteins, the is M. Scholar). that this of has been for complexes the C-terminal cargo binding part of the receptor the data that the molecular from the N-terminal part of the receptor of is of the investigated Pex14p(N)) are a of the binding interaction between Pex5p(F) and a titration was The of Pex14p(N) is that of and Pex14p(N) a complex with the and is to a of Pex14p(N) in the solution with the two are to As in the and to a 1:6 molar and to a molar is with of the titration and is by the gel also a 1:6 molar The structure of Pex5p(F) protein in the of from the scattering is shown in It was by a to the data in the scattering discrepancy is in The model a domain, which may to the C-terminal part of Pex5p and an yielded models of the complex, which the scattering profiles A model in that the complex an conformation in The of the model is to the of Pex5p(F) that are no structural upon complex formation with Pex14p(N) and The of this model with the of that models have The model of the complex binding sites of Pex14p(N) The results of the suggest that the structure of Pex5p(F) remains extended in complex with Pex14p(N) and a the was to a model of the complex by of the data. yielded and the is shown in The of the model is to the from the model the of of the The of N terminus of Pex5p(F) in the complex remains the Pex14p(N) are bound to the N-terminal of The Pex14p(N) the of the complex in intermingled with that of the N terminus of At the the C-terminal domain of Pex5p(F) a structural data (5Stanley W.A. Fodor K. Marti-Renom M.A. Schliebs W. Wilmanns M. FEBS Lett. 2007; 581: 4795-4802Crossref PubMed Scopus (21) Google Scholar, W.A. A. A. Wilmanns M. J. 2004; PubMed Scopus Google model of the complex by The of the in the complex are the as in The and are by the the and an a model of the complex was of the resolution models of the These domains were as the with structure were as of the model of Pex5p(F) was of the C-terminal domain and the N terminus containing Multiple of Biophys. J. 2005; Full Text Full Text PDF PubMed Scopus Google Scholar) from yielded an extended of N-terminal of a to the data were and the which the normalized spatial discrepancy with to the other was model with the model of Pex5p(F) The Biophys. J. 2005; Full Text Full Text PDF PubMed Scopus Google Scholar) was used for of the complex by scattering The N-terminal of Pex5p(F) was as from the and was for two of the and The Pex14p(N) were to have with the binding sites of Pex5p(F) Multiple of yielded models with a stoichiometry The model of the complex the the to that by A with the model in reveals that the two a of the The Pex14p(N) in to the model in a are the of the N terminus. The and conformational of the is in It is that the complex of the the of the models remains The for the and models are and indicating a of the the results a conformation of the N-terminal part of the full-length Pex5p, and were by The results indicate that is The of structure the model an extended The model of the solution structure of human Pex5p(F) and the results indicate that in solution human Pex5p(F) is an monomer the used in with recent studies (15Carvalho A.F. Costa-Rodrigues J. Correia I. Costa Pessoa J. Faria T.Q. Martins C.L. Fransen M. Sá-Miranda C. Azevedo J.E. J. Mol. Biol. 2006; 356: 864-875Crossref PubMed Scopus (68) Google Scholar, 16Costa-Rodrigues J. Carvalho A.F. Fransen M. Hambruch E. Schliebs W. Sá-Miranda C. Azevedo J.E. J. Biol. Chem. 2005; 280: 24404-24411Abstract Full Text Full Text PDF PubMed Scopus (41) Google Scholar). Furthermore, the from reveals that the unfolded N-terminal and the C-terminal TPR domain are in The Pex5p(F) was also by electron microscopy W. J. B. Dodt G. Kunau W.H. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar) with titration by and SLS, which to a stoichiometry of These results are in with and titration of the interaction of Pex14p with which proposed complexes J. Dodt G. Kirchberg K. Wegner A. Nastainczyk W. Kunau W.H. Schliebs W. J. Biol. Chem. 2001; 276: 34524-34529Abstract Full Text Full Text PDF PubMed Scopus (98) Google Scholar, 9Otera H. Setoguchi K. Hamasaki M. Kumashiro T. Shimizu N. Fujiki Y. Mol. Cell. 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