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| | <StructureSection load='2vh1' size='340' side='right'caption='[[2vh1]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='2vh1' size='340' side='right'caption='[[2vh1]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vh1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vh1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VH1 FirstGlance]. <br> |
| - | </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=2vh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vh1 OCA], [https://pdbe.org/2vh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vh1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vh1 ProSAT]</span></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]] 2.7Å</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=2vh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vh1 OCA], [https://pdbe.org/2vh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vh1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vh1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FTSQ_ECOLI FTSQ_ECOLI] Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.[HAMAP-Rule:MF_00911]<ref>PMID:17185541</ref> <ref>PMID:19233928</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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blaauwen, T den]]
| + | [[Category: Ind A]] |
| - | [[Category: Ent, F van den]]
| + | [[Category: Lowe J]] |
| - | [[Category: Ind, A]] | + | [[Category: Naninga N]] |
| - | [[Category: Lowe, J]] | + | [[Category: Veprintsev D]] |
| - | [[Category: Naninga, N]] | + | [[Category: Vinkenvleugel T]] |
| - | [[Category: Veprintsev, D]] | + | [[Category: West P]] |
| - | [[Category: Vinkenvleugel, T]] | + | [[Category: Den Blaauwen T]] |
| - | [[Category: West, P]] | + | [[Category: Van den Ent F]] |
| - | [[Category: Cell cycle]] | + | |
| - | [[Category: Cell division]] | + | |
| - | [[Category: Ftsq]]
| + | |
| - | [[Category: Inner membrane]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Potra]]
| + | |
| - | [[Category: Septation]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
FTSQ_ECOLI Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.[HAMAP-Rule:MF_00911][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
Bacterial cytokinesis requires the divisome, a complex of proteins that co-ordinates the invagination of the cytoplasmic membrane, inward growth of the peptidoglycan layer and the outer membrane. Assembly of the cell division proteins is tightly regulated and the order of appearance at the future division site is well organized. FtsQ is a highly conserved component of the divisome among bacteria that have a cell wall, where it plays a central role in the assembly of early and late cell division proteins. Here, we describe the crystal structure of the major, periplasmic domain of FtsQ from Escherichia coli and Yersinia enterocolitica. The crystal structure reveals two domains; the alpha-domain has a striking similarity to polypeptide transport-associated (POTRA) domains and the C-terminal beta-domain forms an extended beta-sheet overlaid by two, slightly curved alpha-helices. Mutagenesis experiments demonstrate that two functions of FtsQ, localization and recruitment, occur in two separate domains. Proteins that localize FtsQ need the second beta-strand of the POTRA domain and those that are recruited by FtsQ, like FtsL/FtsB, require the surface formed by the tip of the last alpha-helix and the two C-terminal beta-strands. Both domains act together to accomplish the role of FtsQ in linking upstream and downstream cell division proteins within the divisome.
Structural and mutational analysis of the cell division protein FtsQ.,van den Ent F, Vinkenvleugel TM, Ind A, West P, Veprintsev D, Nanninga N, den Blaauwen T, Lowe J Mol Microbiol. 2008 Apr;68(1):110-23. Epub 2008 Feb 26. PMID:18312270[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ D'Ulisse V, Fagioli M, Ghelardini P, Paolozzi L. Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. Microbiology. 2007 Jan;153(Pt 1):124-38. doi: 10.1099/mic.0.2006/000265-0. PMID:17185541 doi:http://dx.doi.org/10.1099/mic.0.2006/000265-0
- ↑ Gonzalez MD, Beckwith J. Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. J Bacteriol. 2009 Apr;191(8):2815-25. doi: 10.1128/JB.01597-08. Epub 2009 Feb 20. PMID:19233928 doi:http://dx.doi.org/10.1128/JB.01597-08
- ↑ van den Ent F, Vinkenvleugel TM, Ind A, West P, Veprintsev D, Nanninga N, den Blaauwen T, Lowe J. Structural and mutational analysis of the cell division protein FtsQ. Mol Microbiol. 2008 Apr;68(1):110-23. Epub 2008 Feb 26. PMID:18312270 doi:http://dx.doi.org/10.1111/j.1365-2958.2008.06141.x
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