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| - | ==FTSZ B. SUBTILIS== | + | ==FtsZ B. subtilis== |
| - | <StructureSection load='2vam' size='340' side='right' caption='[[2vam]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='2vam' size='340' side='right'caption='[[2vam]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vam]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VAM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VAM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vam]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VAM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vam OCA], [http://pdbe.org/2vam PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vam RCSB], [http://www.ebi.ac.uk/pdbsum/2vam PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vam ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vam OCA], [https://pdbe.org/2vam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vam RCSB], [https://www.ebi.ac.uk/pdbsum/2vam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vam ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FTSZ_BACSU FTSZ_BACSU]] 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.<ref>PMID:15317782</ref> <ref>PMID:16159787</ref> | + | [https://www.uniprot.org/uniprot/FTSZ_BACSU FTSZ_BACSU] 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.<ref>PMID:15317782</ref> <ref>PMID:16159787</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/2vam_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/2vam_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | ==See Also== | | ==See Also== |
| - | *[[Cell division protein Ftsz|Cell division protein Ftsz]] | + | *[[Cell division protein 3D structures|Cell division protein 3D structures]] |
| - | *[[Tubulin|Tubulin]]
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Lowe, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Oliva, M A]] | + | [[Category: Lowe J]] |
| - | [[Category: Bacterial cell division protein]] | + | [[Category: Oliva MA]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Gtp-binding]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Polymerization]]
| + | |
| - | [[Category: Septation]]
| + | |
| - | [[Category: Tubulin homolog]]
| + | |
| Structural highlights
Function
FTSZ_BACSU 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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Anderson DE, Gueiros-Filho FJ, Erickson HP. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J Bacteriol. 2004 Sep;186(17):5775-81. PMID:15317782 doi:http://dx.doi.org/10.1128/JB.186.17.5775-5781.2004
- ↑ Jensen SO, Thompson LS, Harry EJ. Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly. J Bacteriol. 2005 Sep;187(18):6536-44. PMID:16159787 doi:http://dx.doi.org/10.1128/JB.187.18.6536-6544.2005
- ↑ Oliva MA, Trambaiolo D, Lowe J. Structural insights into the conformational variability of FtsZ. J Mol Biol. 2007 Nov 9;373(5):1229-42. Epub 2007 Aug 29. PMID:17900614 doi:10.1016/j.jmb.2007.08.056
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