2vap: Difference between revisions
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'''FTSZ GDP M. JANNASCHII''' | '''FTSZ GDP M. JANNASCHII''' | ||
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[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: Oliva, M A.]] | [[Category: Oliva, M A.]] | ||
[[Category: | [[Category: Bacterial cell division protein]] | ||
[[Category: | [[Category: Cell cycle]] | ||
[[Category: | [[Category: Cell division]] | ||
[[Category: | [[Category: Gtp-binding]] | ||
[[Category: | [[Category: Gtpase]] | ||
[[Category: | [[Category: Nucleotide-binding]] | ||
[[Category: | [[Category: Polymerization]] | ||
[[Category: | [[Category: Septation]] | ||
[[Category: | [[Category: Tubulin homolog]] | ||
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Revision as of 18:31, 4 May 2008
FTSZ GDP M. JANNASCHII
OverviewOverview
FtsZ is a prokaryotic homologue of the eukaryotic cytoskeletal protein tubulin and plays a central role in prokaryotic cell division. Both FtsZ and tubulin are known to pass through cycles of polymerization and depolymerization, but the structural mechanisms underlying this cycle remain to be determined. Comparison of tubulin structures obtained in different states has led to a model in which the tubulin monomer undergoes a conformational switch between a "straight" form found in the walls of microtubules and a "curved" form associated with depolymerization, and it was proposed recently that this model may apply also to FtsZ. Here, we present new structures of FtsZ from47 Aquifex aeolicus,47 Bacillus subtilis, Methanococcus jannaschii and Pseudomonas aeruginosa that provide strong constraints on any proposed role for a conformational switch in the FtsZ monomer. By comparing the full range of FtsZ structures determined in different crystal forms and nucleotide states, and in the presence or in the absence of regulatory proteins, we find no evidence of a conformational change involving domain movement. Our new structural data make it clear that the previously proposed straight and curved conformations of FtsZ were related to inter-species differences in domain orientation rather than two interconvertible conformations. We propose a new model in which lateral interactions help determine the curvature of protofilaments.
About this StructureAbout this Structure
2VAP is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into the conformational variability of FtsZ., Oliva MA, Trambaiolo D, Lowe J, J Mol Biol. 2007 Nov 9;373(5):1229-42. Epub 2007 Aug 29. PMID:17900614 Page seeded by OCA on Sun May 4 18:30:59 2008