2qa5
From Proteopedia
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Crystal structure of Sept2 G-domain
Overview
Septins are GTP-binding proteins that assemble into homo- and, hetero-oligomers and filaments. Although they have key roles in various, cellular processes, little is known concerning the structure of septin, subunits or the organization and polarity of septin complexes. Here we, present the structures of the human SEPT2 G domain and the heterotrimeric, human SEPT2-SEPT6-SEPT7 complex. The structures reveal a universal bipolar, polymer building block, composed of an extended G domain, which forms, oligomers and filaments by conserved interactions between adjacent, nucleotide-binding sites and/or the amino- and carboxy-terminal, extensions. Unexpectedly, X-ray crystallography and electron microscopy, showed that the predicted coiled coils are not involved in or required for, complex and/or filament formation. The asymmetrical heterotrimers, associate head-to-head to form a hexameric unit that is nonpolarized along, the filament axis but is rotationally asymmetrical. The architecture of, septin filaments differs fundamentally from that of other cytoskeletal, structures.
About this Structure
2QA5 is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Structural insight into filament formation by mammalian septins., Sirajuddin M, Farkasovsky M, Hauer F, Kuhlmann D, Macara IG, Weyand M, Stark H, Wittinghofer A, Nature. 2007 Jul 18;. PMID:17637674
Page seeded by OCA on Thu Jan 31 10:58:21 2008
