3t5d | pdb_00003t5d
Crystal structure of Septin 7 in complex with GDP
Structural highlights
Function[SEPT7_HUMAN] Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements.[1] [2] Publication Abstract from PubMedAbstract 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. Structural and biochemical properties of Sept7, a unique septin required for filament formation.,Zent E, Vetter I, Wittinghofer A Biol Chem. 2011 Aug;392(8-9):791-7. PMID:21824007[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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