Promiscuous interactions of human septins: the GTP binding domain of SEPT7 forms filaments within the crystal |
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| Authors: | Serrão Vitor Hugo Balasco Alessandro Fernando Caldas Victor Emanoel Armini Marçal Rafaela Leite Pereira Humberto D'Muniz Thiemann Otavio Henrique Garratt Richard Charles |
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| Institution: | Centro de Biotecnologia Molecular Estrutural, Instituto de Física de São Carlos, Universidade de São Paulo, Brazil |
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| Abstract: | 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.Structured summary of protein interactionsSEPT7G and SEPT7Gbind by X-ray crystallography (View interaction).SEPT7 G and SEPT7 Gbind by molecular sieving (View interaction). |
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| Keywords: | Septin SEPT7 GTP-binding domain Filament Promiscuous interaction Subunit interface |
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