View source for 6scp


==Cell Division Protein SepF in complex with C-terminal domain of FtsZ==
<StructureSection load='6scp' size='340' side='right'caption='[[6scp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6scp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Corgl Corgl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SCP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sepF, Cgl2152 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=196627 CORGL])</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=6scp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scp OCA], [http://pdbe.org/6scp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6scp RCSB], [http://www.ebi.ac.uk/pdbsum/6scp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6scp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. Here we investigate the physiological function of Corynebacterium glutamicum SepF, the only cell division-associated protein from Actinobacteria known to interact with the conserved C-terminal tail of FtsZ. We show an essential interdependence of FtsZ and SepF for formation of a functional Z-ring in C. glutamicum. The crystal structure of the SepF-FtsZ complex reveals a hydrophobic FtsZ-binding pocket, which defines the SepF homodimer as the functional unit, and suggests a reversible oligomerization interface. FtsZ filaments and lipid membranes have opposing effects on SepF polymerization, indicating that SepF has multiple roles at the cell division site, involving FtsZ bundling, Z-ring tethering and membrane reshaping activities that are needed for proper Z-ring assembly and function.

Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum.,Sogues A, Martinez M, Gaday Q, Ben Assaya M, Grana M, Voegele A, VanNieuwenhze M, England P, Haouz A, Chenal A, Trepout S, Duran R, Wehenkel AM, Alzari PM Nat Commun. 2020 Apr 2;11(1):1641. doi: 10.1038/s41467-020-15490-8. PMID:32242019<ref>PMID:32242019</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6scp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Corgl]]
[[Category: Large Structures]]
[[Category: Alzari, P M]]
[[Category: Sogues, A]]
[[Category: Wehenkel, A M]]
[[Category: Cell cycle]]
[[Category: Cell division protein]]