What question did this study set out to answer?

Determine the three-dimensional structure and stability mechanisms of the two-chain complex produced by thermolysin cleavage of the antimicrobial peptide microcin J25.

March 27, 2004Biochemistry

Structure of Thermolysin Cleaved Microcin J25: Extreme Stability of a Two-Chain Antimicrobial Peptide Devoid of Covalent Links,

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Authors

KRK. Johan RosengrenThe University of Queensland ABAlain BlondCentre National de la Recherche Scientifique CACarlos AfonsoCentre National de la Recherche Scientifique

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Implication

Structural analysis reveals extreme stability in thermolysin-cleaved microcin J25 without covalent links, highlighting unique mechanical entrapment in lasso-like peptides.

Key Points

Determine the three-dimensional structure and stability mechanisms of the two-chain complex produced by thermolysin cleavage of the antimicrobial peptide microcin J25.
Treated the 21-amino-acid antimicrobial peptide microcin J25 with thermolysin to cleave the Phe10-Val11 amide bond.
Characterized structural properties and chain association using nuclear magnetic resonance (NMR) spectroscopy, mass spectrometry, and simulated annealing calculations.
NMR and simulated annealing resolved a rigid core formed by the N-terminal octapeptide ring and the threaded C-terminal tail, while the cleaved Phe10 and Val11 termini remained disordered in solution.
The two cleaved chains remained stably associated in both solution and gas phases under denaturing conditions without any disulfide or interchain covalent bonds.
Entrapment of the C-terminal tail within the ring was stabilized by hydrogen-bonded beta-sheets, hydrophobic contacts, and steric blocking by bulky Phe19 and Tyr20 side chains.

Cite This Study

Rosengren et al. (2004) studied this question.

synapsesocial.com/papers/69dd7c6580eea7d3f699cea3 https://doi.org/10.1021/bi0361261

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Implication

Structural analysis reveals extreme stability in thermolysin-cleaved microcin J25 without covalent links, highlighting unique mechanical entrapment in lasso-like peptides.

Structure of Thermolysin Cleaved Microcin J25: Extreme Stability of a Two-Chain Antimicrobial Peptide Devoid of Covalent Links,

Discussion

Member takes

Implication

Key Points

Cite This Study

Structure of Thermolysin Cleaved Microcin J25: Extreme Stability of a Two-Chain Antimicrobial Peptide Devoid of Covalent Links,

Discussion

Member takes

Implication

Key Points

Cite This Study

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