6scq: Difference between revisions
New page: '''Unreleased structure''' The entry 6scq is ON HOLD Authors: Sogues, A., Wehenkel, A.M., Alzari, P.M. Description: Cell Division Protein SepF in complex with C-terminal domain of FtsZ... |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Cell Division Protein SepF in complex with C-terminal domain of FtsZ== | |||
<StructureSection load='6scq' size='340' side='right'caption='[[6scq]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6scq]] 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=6SCQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SCQ FirstGlance]. <br> | |||
</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=6scq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scq OCA], [http://pdbe.org/6scq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6scq RCSB], [http://www.ebi.ac.uk/pdbsum/6scq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6scq 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6scq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Corgl]] | |||
[[Category: Large Structures]] | |||
[[Category: Alzari, P M]] | |||
[[Category: Sogues, A]] | [[Category: Sogues, A]] | ||
[[Category: Wehenkel, A | [[Category: Wehenkel, A M]] | ||
[[Category: | [[Category: Cell cycle]] | ||
[[Category: Cell division protein]] | |||
Latest revision as of 14:25, 23 September 2020
Cell Division Protein SepF in complex with C-terminal domain of FtsZCell Division Protein SepF in complex with C-terminal domain of FtsZ
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||