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1w5e
From Proteopedia
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FTSZ W319Y MUTANT, P1 (M. JANNASCHII)
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, exchangeable, explaining why, in this filament, nucleotide hydrolysis is, the rate-limiting step during FtsZ polymerization. Furthermore, crystal, structures of FtsZ in different nucleotide states reveal notably few, differences.
About this Structure
1W5E is a Single protein structure of sequence from Methanocaldococcus jannaschii with GTP as ligand. Known structural/functional Site: . 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 Dec 18 18:31:11 2007
