6sat: Difference between revisions
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<StructureSection load='6sat' size='340' side='right'caption='[[6sat]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='6sat' size='340' side='right'caption='[[6sat]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6sat]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SAT OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[6sat]] is a 4 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=6SAT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SAT FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | </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=6sat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sat OCA], [http://pdbe.org/6sat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sat RCSB], [http://www.ebi.ac.uk/pdbsum/6sat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sat ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FTSZ_CORGL FTSZ_CORGL]] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909] | [[http://www.uniprot.org/uniprot/FTSZ_CORGL FTSZ_CORGL]] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909] | ||
<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> | |||
</div> | |||
<div class="pdbe-citations 6sat" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cell division protein 3D structures|Cell division protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Corgl]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alzari, P M]] | [[Category: Alzari, P M]] | ||
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
Function[FTSZ_CORGL] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909] 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. See AlsoReferences
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