2mmv: Difference between revisions

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 ==ZapA mutant dimer from Geobacillus stearothermophilus==
-<StructureSection load='2mmv' size='340' side='right' caption='[[2mmv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2mmv' size='340' side='right'caption='[[2mmv]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2mmv]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MMV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2mmv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MMV FirstGlance]. <br>
-</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=2mmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmv OCA], [http://pdbe.org/2mmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mmv RCSB], [http://www.ebi.ac.uk/pdbsum/2mmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmv ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmv OCA], [https://pdbe.org/2mmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mmv RCSB], [https://www.ebi.ac.uk/pdbsum/2mmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A0A078N0N2_GEOSE A0A078N0N2_GEOSE]] Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.[HAMAP-Rule:MF_02013]  Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division (By similarity).[SAAS:SAAS00206040]
+[https://www.uniprot.org/uniprot/A0A078N0N2_GEOSE A0A078N0N2_GEOSE] Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.[HAMAP-Rule:MF_02013]  Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division (By similarity).[SAAS:SAAS00206040]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacterial division begins with the formation of a contractile protein ring at midcell, which constricts the bacterial envelope to generate two daughter cells. The central component of the division ring is FtsZ, a tubulin-like protein capable of self-assembling into filaments which further associate into a higher order structure known as the Z ring. Proteins that bind to FtsZ play a crucial role in the formation and regulation of the Z ring. One such protein is ZapA, a widely conserved 21 kDa homodimeric protein that associates with FtsZ filaments and promotes their bundling. Although ZapA was discovered more than a decade ago, the structural details of its interaction with FtsZ remain unknown. In this work, backbone and side chain NMR assignments for the Geobacillus stearothermophilus ZapA homodimer are described. We titrated FtsZ into (15)N(2)H-ZapA and mapped ZapA residues whose resonances are perturbed upon FtsZ binding. This information provides a structural understanding of the interaction between FtsZ and ZapA.
+Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ.,Nogueira ML, Sforca ML, Chin YK, Mobli M, Handler A, Gorbatyuk VY, Robson SA, King GF, Gueiros-Filho FJ, Zeri AC Biomol NMR Assign. 2015 Oct;9(2):387-91. doi: 10.1007/s12104-015-9615-1. Epub , 2015 May 13. PMID:25967379<ref>PMID:25967379</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2mmv" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Cell division protein|Cell division protein]]
+*[[Cell division protein 3D structures|Cell division protein 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Nogueira, M L]]
+[[Category: Geobacillus stearothermophilus]]
-[[Category: Sforca, M]]
+[[Category: Large Structures]]
-[[Category: Zeri, A]]
+[[Category: Nogueira ML]]
-[[Category: Cell cycle]]
+[[Category: Sforca M]]
-[[Category: Zapa]]
+[[Category: Zeri A]]