1w5f

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spinqualitylabelsall models 1w5f, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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, 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

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

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