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1w5e
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure | + | 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== | ||
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[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cordell, S | + | [[Category: Cordell, S C.]] |
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
| - | [[Category: Oliva, M | + | [[Category: Oliva, M A.]] |
[[Category: GTP]] | [[Category: GTP]] | ||
[[Category: cell division]] | [[Category: cell division]] | ||
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[[Category: z-ring]] | [[Category: z-ring]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:40 2008'' |
Revision as of 13:40, 21 February 2008
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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 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 Thu Feb 21 15:40:40 2008
