2vxy: Difference between revisions

Revision as of 21:12, 19 September 2018

The structure of FTsZ from Bacillus subtilis at 1.7A resolution

Structural highlights

2vxy is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	CIT, K
Related:	2vam
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FTSZ_BACSU] 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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

FtsZ is an essential bacterial guanosine triphosphatase and homolog of mammalian beta-tubulin that polymerizes and assembles into a ring to initiate cell division. We have created a class of small synthetic antibacterials, exemplified by PC190723, which inhibits FtsZ and prevents cell division. PC190723 has potent and selective in vitro bactericidal activity against staphylococci, including methicillin- and multi-drug-resistant Staphylococcus aureus. The putative inhibitor-binding site of PC190723 was mapped to a region of FtsZ that is analogous to the Taxol-binding site of tubulin. PC190723 was efficacious in an in vivo model of infection, curing mice infected with a lethal dose of S. aureus. The data validate FtsZ as a target for antibacterial intervention and identify PC190723 as suitable for optimization into a new anti-staphylococcal therapy.

An inhibitor of FtsZ with potent and selective anti-staphylococcal activity.,Haydon DJ, Stokes NR, Ure R, Galbraith G, Bennett JM, Brown DR, Baker PJ, Barynin VV, Rice DW, Sedelnikova SE, Heal JR, Sheridan JM, Aiwale ST, Chauhan PK, Srivastava A, Taneja A, Collins I, Errington J, Czaplewski LG Science. 2008 Sep 19;321(5896):1673-5. PMID:18801997^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Anderson DE, Gueiros-Filho FJ, Erickson HP. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J Bacteriol. 2004 Sep;186(17):5775-81. PMID:15317782 doi:https://dx.doi.org/10.1128/JB.186.17.5775-5781.2004
↑ Jensen SO, Thompson LS, Harry EJ. Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly. J Bacteriol. 2005 Sep;187(18):6536-44. PMID:16159787 doi:https://dx.doi.org/10.1128/JB.187.18.6536-6544.2005
↑ Haydon DJ, Stokes NR, Ure R, Galbraith G, Bennett JM, Brown DR, Baker PJ, Barynin VV, Rice DW, Sedelnikova SE, Heal JR, Sheridan JM, Aiwale ST, Chauhan PK, Srivastava A, Taneja A, Collins I, Errington J, Czaplewski LG. An inhibitor of FtsZ with potent and selective anti-staphylococcal activity. Science. 2008 Sep 19;321(5896):1673-5. PMID:18801997 doi:321/5896/1673

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Anderson DE, Gueiros-Filho FJ, Erickson HP. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J Bacteriol. 2004 Sep;186(17):5775-81. PMID:15317782 doi:https://dx.doi.org/10.1128/JB.186.17.5775-5781.2004

[2] Jensen SO, Thompson LS, Harry EJ. Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly. J Bacteriol. 2005 Sep;187(18):6536-44. PMID:16159787 doi:https://dx.doi.org/10.1128/JB.187.18.6536-6544.2005

[3] Haydon DJ, Stokes NR, Ure R, Galbraith G, Bennett JM, Brown DR, Baker PJ, Barynin VV, Rice DW, Sedelnikova SE, Heal JR, Sheridan JM, Aiwale ST, Chauhan PK, Srivastava A, Taneja A, Collins I, Errington J, Czaplewski LG. An inhibitor of FtsZ with potent and selective anti-staphylococcal activity. Science. 2008 Sep 19;321(5896):1673-5. PMID:18801997 doi:321/5896/1673

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-==THE STRUCTURE OF FTSZ FROM BACILLUS SUBTILIS AT 1.7A RESOLUTION==
+==The structure of FTsZ from Bacillus subtilis at 1.7A resolution==
 <StructureSection load='2vxy' size='340' side='right' caption='[[2vxy]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vxy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vxy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXY FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vam|2vam]]</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=2vxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxy OCA], [http://pdbe.org/2vxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxy RCSB], [http://www.ebi.ac.uk/pdbsum/2vxy PDBsum]</span></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=2vxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxy OCA], [http://pdbe.org/2vxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxy RCSB], [http://www.ebi.ac.uk/pdbsum/2vxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxy ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vx/2vxy_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vx/2vxy_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Cell division protein Ftsz|Cell division protein Ftsz]]
+*[[Cell division protein|Cell division protein]]
 *[[Tubulin|Tubulin]]
 == References ==
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Vibrio subtilis ehrenberg 1835]]
 [[Category: Aiwale, S T]]
 [[Category: Baker, P J]]
@@ Line 60: / Line 61: @@
 [[Category: Cell division]]
 [[Category: Cell division protein]]
+[[Category: Cytoplasm]]
 [[Category: Ftsz]]
 [[Category: Gtp-binding]]
 [[Category: Nucleotide-binding]]
 [[Category: Septation]]

2vxy: Difference between revisions

Revision as of 21:12, 19 September 2018

The structure of FTsZ from Bacillus subtilis at 1.7A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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