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New page: ==ZapC cell division regulator from E. coli== <StructureSection load='5fo3' size='340' side='right' caption='5fo3, resolution 2.90Å' scene=''> == Structural highli... |
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==ZapC cell division regulator from E. coli== | ==ZapC cell division regulator from E. coli== | ||
<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. 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 [ | <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=' | </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'>[ | <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 == | ||
[ | [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;"> | |||
== 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<ref>PMID:26619764</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5fo3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cell division protein 3D structures|Cell division protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Kureisaite-Ciziene D]] | ||
[[Category: | [[Category: Lowe J]] | ||
[[Category: | [[Category: Ortiz C]] | ||
[[Category: | [[Category: Schmitz F]] | ||
[[Category: | [[Category: Vicente M]] | ||
Latest revision as of 10:00, 19 July 2023
ZapC cell division regulator from E. coliZapC cell division regulator from E. coli
Structural highlights
FunctionZAPC_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 PubMedBacterial 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 AlsoReferences
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