期刊
BIOLOGICAL CHEMISTRY
卷 392, 期 8-9, 页码 791-797出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2011.082
关键词
cytoskeleton; filament; GTP-binding protein; septin; X-ray crystallography
资金
- International Max Planck Research School for Chemical Biology
Septins constitute a family of conserved guanine nucleotide binding proteins found in a wide range of organisms from fungi to mammals. Members of the family share a canonical G-domain with N- and C-terminal extensions. G-domains assemble into hetero-oligomeric complexes which form non-polarised filaments or rings. Linear filaments are formed between the G-domains using either the guanine nucleotide binding site (G interface) or N- and C-terminal extensions (NC interface). Sept7 is a unique among the 13 human septins in that it occupies the ends of hexameric building blocks which assemble into non-polarised filaments. To gain insight into its particular properties we performed structural and biochemical studies on Sept7. We solved the crystal structure of a Sept7 dimer in the GDP-bound state. The structure and biochemistry of Sept7 provide new insights into the dynamics of the G interface and outline the differences in the properties of Sept7 compared to the members of group 2 septins.
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