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| [[Image:1w5e.gif|left|200px]] | | {{Seed}} |
| | [[Image:1w5e.png|left|200px]] |
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| {{STRUCTURE_1w5e| PDB=1w5e | SCENE= }} | | {{STRUCTURE_1w5e| PDB=1w5e | SCENE= }} |
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| '''FTSZ W319Y MUTANT, P1 (M. JANNASCHII)'''
| | ===FTSZ W319Y MUTANT, P1 (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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15558053}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15558053 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15558053}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tubulin]] | | [[Category: Tubulin]] |
| [[Category: Z-ring]] | | [[Category: Z-ring]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:11:08 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:25:51 2008'' |
