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| | <StructureSection load='5fo3' size='340' side='right'caption='[[5fo3]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='5fo3' size='340' side='right'caption='[[5fo3]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fo3]] is a 2 chain structure with sequence from [http://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=5FO3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FO3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fo3]] 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=5FO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FO3 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.9Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fo3 OCA], [http://pdbe.org/5fo3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fo3 RCSB], [http://www.ebi.ac.uk/pdbsum/5fo3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fo3 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5fo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fo3 OCA], [https://pdbe.org/5fo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fo3 RCSB], [https://www.ebi.ac.uk/pdbsum/5fo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fo3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ZAPC_ECOLI ZAPC_ECOLI]] Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.[HAMAP-Rule:MF_00906]<ref>PMID:21216995</ref> <ref>PMID:21216997</ref> | + | [https://www.uniprot.org/uniprot/ZAPC_ECOLI ZAPC_ECOLI] Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.[HAMAP-Rule:MF_00906]<ref>PMID:21216995</ref> <ref>PMID:21216997</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kureisaite-Ciziene, D]] | + | [[Category: Kureisaite-Ciziene D]] |
| - | [[Category: Lowe, J]] | + | [[Category: Lowe J]] |
| - | [[Category: Ortiz, C]] | + | [[Category: Ortiz C]] |
| - | [[Category: Schmitz, F]] | + | [[Category: Schmitz F]] |
| - | [[Category: Vicente, M]] | + | [[Category: Vicente M]] |
| - | [[Category: Bacterial cell division]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Ftsz]]
| + | |
| - | [[Category: Z-ring associated protein c]]
| + | |
| Structural highlights
Function
ZAPC_ECOLI Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.[HAMAP-Rule:MF_00906][1] [2]
Publication Abstract from PubMed
Bacterial cell division involves a contractile ring that organises downstream proteins at the division site and which contains the tubulin homologue FtsZ. ZapC has been discovered as a non-essential regulator of FtsZ. It localises to the septal ring and deletion of zapC leads to a mild phenotype, while overexpression inhibits cell division. Interference with cell division is facilitated by an interaction with FtsZ. Here, we present the 2.9A crystal structure of ZapC from Escherichia coli. ZapC forms a dimer and comprises two domains that belong to the Royal superfamily of which many members bind methylated arginines or lysines. ZapC contains an N-terminal chromo-like domain and a Tudor-like C-terminal domain. We show by ITC that ZapC binds the C-terminal tail of FtsZ.
Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.,Ortiz C, Kureisaite-Ciziene D, Schmitz F, McLaughlin SH, Vicente M, Lowe J FEBS Lett. 2015 Nov 30. pii: S0014-5793(15)01034-0. doi:, 10.1016/j.febslet.2015.11.030. PMID:26619764[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Durand-Heredia JM, Yu HH, De Carlo S, Lesser CF, Janakiraman A. Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J Bacteriol. 2011 Mar;193(6):1405-13. doi: 10.1128/JB.01258-10. Epub 2011 Jan 7. PMID:21216995 doi:http://dx.doi.org/10.1128/JB.01258-10
- ↑ Hale CA, Shiomi D, Liu B, Bernhardt TG, Margolin W, Niki H, de Boer PA. Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. J Bacteriol. 2011 Mar;193(6):1393-404. doi: 10.1128/JB.01245-10. Epub 2011 Jan 7. PMID:21216997 doi:http://dx.doi.org/10.1128/JB.01245-10
- ↑ Ortiz C, Kureisaite-Ciziene D, Schmitz F, McLaughlin SH, Vicente M, Lowe J. Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli. FEBS Lett. 2015 Nov 30. pii: S0014-5793(15)01034-0. doi:, 10.1016/j.febslet.2015.11.030. PMID:26619764 doi:http://dx.doi.org/10.1016/j.febslet.2015.11.030
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