Key result
The GTP-binding domain of human septin 7 forms filaments within the crystal lattice using both G and NC interfaces, suggesting these interfaces are necessary but insufficient for correct assembly.
The structural analysis of SEPT7G reveals promiscuous interactions at the NC interface, providing insight into the assembly and diversity of septin hetero-polymers.
Does not yet alter clinical practice; leaves open septin roles in cellular and disease models pending functional validation.
We describe the purification, crystallization and structure for the GTP-binding domain of human septin 7 (SEPT7G). We show that it forms filaments within the crystal lattice which employ both the G and NC interfaces, similar to those seen in the hetero-filament of SEPT2/6/7. The NC interface is considered promiscuous as it is absent from the hetero-filament. Such promiscuity could provide the potential for permuting monomers along a filament in order to generate diversity in hetero-polymers. On the other hand, our results suggest that the G and NC interfaces may be necessary but insufficient for determining correct hetero-filament assembly.
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Serrão et al. (2011) studied this question. Purification and crystallization of human septin 7 GTP-binding domain (SEPT7G) was evaluated on Crystal structure and filament formation. The GTP-binding domain of human septin 7 forms filaments within the crystal lattice using both G and NC interfaces, suggesting these interfaces are necessary but insufficient for correct assembly.
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