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| | <StructureSection load='1w5f' size='340' side='right'caption='[[1w5f]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1w5f' size='340' side='right'caption='[[1w5f]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w5f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W5F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w5f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W5F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fsz|1fsz]], [[1w58|1w58]], [[1w59|1w59]], [[1w5a|1w5a]], [[1w5b|1w5b]], [[1w5e|1w5e]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1w5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w5f OCA], [https://pdbe.org/1w5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w5f RCSB], [https://www.ebi.ac.uk/pdbsum/1w5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w5f ProSAT]</span></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=1w5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w5f OCA], [https://pdbe.org/1w5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w5f RCSB], [https://www.ebi.ac.uk/pdbsum/1w5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w5f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FTSZ_THEMA FTSZ_THEMA]] 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:9605973</ref>
| + | [https://www.uniprot.org/uniprot/FTSZ_THEMA FTSZ_THEMA] 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:9605973</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cordell, S C]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Lowe, J]] | + | [[Category: Cordell SC]] |
| - | [[Category: Oliva, M A]] | + | [[Category: Lowe J]] |
| - | [[Category: Cell division]] | + | [[Category: Oliva MA]] |
| - | [[Category: Cell-division protein]]
| + | |
| - | [[Category: Domain swapped]]
| + | |
| - | [[Category: Filament]]
| + | |
| - | [[Category: Ftsz]]
| + | |
| - | [[Category: Gtp-binding]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Multigene family]]
| + | |
| - | [[Category: Septation]]
| + | |
| - | [[Category: Tubulin]]
| + | |
| - | [[Category: Z-ring]]
| + | |
| Structural highlights
Function
FTSZ_THEMA 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]
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
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lu C, Stricker J, Erickson HP. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima--quantitation, GTP hydrolysis, and assembly. Cell Motil Cytoskeleton. 1998;40(1):71-86. PMID:9605973 doi:<71::AID-CM7>3.0.CO;2-I http://dx.doi.org/10.1002/(SICI)1097-0169(1998)40:1<71::AID-CM7>3.0.CO;2-I
- ↑ Oliva MA, Cordell SC, Lowe J. Structural insights into FtsZ protofilament formation. Nat Struct Mol Biol. 2004 Dec;11(12):1243-50. Epub 2004 Nov 21. PMID:15558053 doi:10.1038/nsmb855
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