1w5a

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{{STRUCTURE_1w5a| PDB=1w5a | SCENE= }}
{{STRUCTURE_1w5a| PDB=1w5a | SCENE= }}
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'''FTSZ DIMER, MGGTP SOAK (M. JANNASCHII)'''
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===FTSZ DIMER, MGGTP SOAK (M. JANNASCHII)===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15558053}}
==About this Structure==
==About this Structure==
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[[Category: Tubulin]]
[[Category: Tubulin]]
[[Category: Z-ring]]
[[Category: Z-ring]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:10:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:56:30 2008''

Revision as of 04:56, 28 July 2008

Template:STRUCTURE 1w5a

FTSZ DIMER, MGGTP SOAK (M. JANNASCHII)

Template:ABSTRACT PUBMED 15558053

About this Structure

1W5A is a Single protein structure of sequence from Methanocaldococcus jannaschii. 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 Mon Jul 28 07:56:30 2008

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