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1w5f
From Proteopedia
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FTSZ, T7 MUTATED, DOMAIN SWAPPED (T. MARITIMA)
Overview
The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure, essential for bacterial cell division. We have used refolded FtsZ to, crystallize a tubulin-like protofilament. The N- and C-terminal domains of, two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A, domain-swapped structure of FtsZ and biochemical data on purified N- and, C-terminal domains show that they are independent. This leads to a model, of how FtsZ and tubulin polymerization evolved by fusing two domains. In, polymerized tubulin, the nucleotide-binding pocket is occluded, which, leads to nucleotide exchange being the rate-limiting step and to dynamic, instability. In our FtsZ filament structure the nucleotide is, ... [(full description)]
About this Structure
1W5F is a [Single protein] structure of sequence from [Thermotoga maritima] with MG and G2P as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structural insights into FtsZ protofilament formation., Oliva MA, Cordell SC, Lowe J, Nat Struct Mol Biol. 2004 Dec;11(12):1243-50. Epub 2004 Nov 21. PMID:15558053
Page seeded by OCA on Tue Oct 30 16:25:41 2007
Categories: Single protein | Thermotoga maritima | Cordell, S.C. | Lowe, J. | Oliva, M.A. | G2P | MG | Cell division | Cell-division protein | Complete proteome | Domain swapped | Filament | Ftsz | Gtp-binding | Gtpase | Multigene family | Septation | Tubulin | Z-ring
