2vap

FtsZ GDP M. jannaschii

spinqualitylabelsall models 2vap, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vap is a 1 chain structure with sequence from Metja. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP Related: 1w58, 1w5a, 1w5b, 1fsz, 1w59, 1w5e Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FTSZ1_METJA] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cell division protein Tubulin

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