1w58
From Proteopedia
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==Overview== | ==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, .. | + | 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== | ==About this Structure== | ||
| - | 1W58 is a | + | 1W58 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG and G2P as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W58 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tubulin]] | [[Category: tubulin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:29:10 2007'' |
Revision as of 11:23, 5 November 2007
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FTSZ GMPCPP SOAK I213 (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
1W58 is a Single protein structure of sequence from Methanocaldococcus jannaschii 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 Mon Nov 5 13:29:10 2007
