3q9l - Revision history

OCA at 10:46, 21 February 2024

OCA — Wed, 21 Feb 2024 10:46:38 GMT

←Older revision		Revision as of 10:46, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3q9l' size='340' side='right'caption='[[3q9l]], [[Resolution\|resolution]] 2.34Å' scene=''>		<StructureSection load='3q9l' size='340' side='right'caption='[[3q9l]], [[Resolution\|resolution]] 2.34Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q9L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q9L FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ATP:ADENOSINE~~-~~5-TRIPHOSPHATE'>ATP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.343Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~minD ([https~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=83333 ECOLI])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [https://pdbe.org/3q9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [https://www.ebi.ac.uk/pdbsum/3q9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9l ProSAT]</span></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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [https://pdbe.org/3q9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [https://www.ebi.ac.uk/pdbsum/3q9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9l ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref>	+	[https://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The three Min proteins spatially regulate Z ring positioning in Escherichia coli and are dynamically associated with the membrane. MinD binds to vesicles in the presence of ATP and can recruit MinC or MinE. Biochemical and genetic evidence indicate the binding sites for these two proteins on MinD overlap. Here we solved the structure of a hydrolytic-deficient mutant of MinD truncated for the C-terminal amphipathic helix involved in binding to the membrane. The structure solved in the presence of ATP is a dimer and reveals the face of MinD abutting the membrane. Using a combination of random and extensive site-directed mutagenesis additional residues important for MinE and MinC binding were identified. The location of these residues on the MinD structure confirms that the binding sites overlap and reveals that the binding sites are at the dimer interface and exposed to the cytosol. The location of the binding sites at the dimer interface offers a simple explanation for the ATP dependence of MinC and MinE binding to MinD.	+
-		+
-	Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.,Wu W, Park KT, Holyoak T, Lutkenhaus J Mol Microbiol. 2011 Jan 14. doi: 10.1111/j.1365-2958.2010.07536.x. PMID:21231967<ref>PMID:21231967</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3q9l" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Holyoak, T]]	+	[[Category: Holyoak T]]
-	[[Category: Lutkenhaus, J]]	+	[[Category: Lutkenhaus J]]
-	[[Category: Park, K T]]	+	[[Category: Park K-T]]
-	[[Category: Wu, W]]	+	[[Category: Wu W]]
-	~~[[Category: Atpase]]~~	+
-	~~[[Category: Bacterial cell division inhibitor]]~~	+
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Minc]]~~	+
-	~~[[Category: Mine~~]]	+

OCA at 05:58, 8 June 2022

OCA — Wed, 08 Jun 2022 05:58:56 GMT

←Older revision		Revision as of 05:58, 8 June 2022
Line 1:		Line 1:

	==The structure of the dimeric E.coli MinD-ATP complex==		==The structure of the dimeric E.coli MinD-ATP complex==
-	<StructureSection load='3q9l' size='340' side='right' caption='[[3q9l]], [[Resolution\|resolution]] 2.34Å' scene=''>	+	<StructureSection load='3q9l' size='340' side='right'caption='[[3q9l]], [[Resolution\|resolution]] 2.34Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3Q9L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q9L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">minD ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">minD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [~~http~~://pdbe.org/3q9l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3q9l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9l ProSAT]</span></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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [https://pdbe.org/3q9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [https://www.ebi.ac.uk/pdbsum/3q9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9l ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref>	+	[[https://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Ecoli]]		[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Holyoak, T]]		[[Category: Holyoak, T]]
	[[Category: Lutkenhaus, J]]		[[Category: Lutkenhaus, J]]

OCA at 05:48, 5 August 2016

OCA — Fri, 05 Aug 2016 05:48:38 GMT

←Older revision		Revision as of 05:48, 5 August 2016
Line 1:		Line 1:
		+
	==The structure of the dimeric E.coli MinD-ATP complex==		==The structure of the dimeric E.coli MinD-ATP complex==
	<StructureSection load='3q9l' size='340' side='right' caption='[[3q9l]], [[Resolution\|resolution]] 2.34Å' scene=''>		<StructureSection load='3q9l' size='340' side='right' caption='[[3q9l]], [[Resolution\|resolution]] 2.34Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia coli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q9L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q9L FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">minD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~562 Escherichia coli~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">minD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [http://www.ebi.ac.uk/pdbsum/3q9l 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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [http://pdbe.org/3q9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [http://www.ebi.ac.uk/pdbsum/3q9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9l ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3q9l" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Ecoli]]
	[[Category: Holyoak, T]]		[[Category: Holyoak, T]]
	[[Category: Lutkenhaus, J]]		[[Category: Lutkenhaus, J]]

OCA at 16:16, 25 December 2014

OCA — Thu, 25 Dec 2014 16:16:23 GMT

←Older revision		Revision as of 16:16, 25 December 2014
Line 7:		Line 7:
	<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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [http://www.ebi.ac.uk/pdbsum/3q9l 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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [http://www.ebi.ac.uk/pdbsum/3q9l PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:34, 19 December 2014

OCA — Fri, 19 Dec 2014 10:34:14 GMT

←Older revision		Revision as of 10:34, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3q9l\| PDB=3q9l \| SCENE= }}~~	+	==The structure of the dimeric E.coli MinD-ATP complex==
-	===The structure of the dimeric E.coli MinD-ATP complex===	+	<StructureSection load='3q9l' size='340' side='right' caption='[[3q9l]], [[Resolution\|resolution]] 2.34Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21231967}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3q9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q9L FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">minD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q9l RCSB], [http://www.ebi.ac.uk/pdbsum/3q9l PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The three Min proteins spatially regulate Z ring positioning in Escherichia coli and are dynamically associated with the membrane. MinD binds to vesicles in the presence of ATP and can recruit MinC or MinE. Biochemical and genetic evidence indicate the binding sites for these two proteins on MinD overlap. Here we solved the structure of a hydrolytic-deficient mutant of MinD truncated for the C-terminal amphipathic helix involved in binding to the membrane. The structure solved in the presence of ATP is a dimer and reveals the face of MinD abutting the membrane. Using a combination of random and extensive site-directed mutagenesis additional residues important for MinE and MinC binding were identified. The location of these residues on the MinD structure confirms that the binding sites overlap and reveals that the binding sites are at the dimer interface and exposed to the cytosol. The location of the binding sites at the dimer interface offers a simple explanation for the ATP dependence of MinC and MinE binding to MinD.

-	~~==Function==~~	+	Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.,Wu W, Park KT, Holyoak T, Lutkenhaus J Mol Microbiol. 2011 Jan 14. doi: 10.1111/j.1365-2958.2010.07536.x. PMID:21231967<ref>PMID:21231967</ref>
-	~~[[http://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for~~ the ~~correct placement~~ of the ~~division site. Cell division inhibitors MinC and~~ MinD ~~act in concert to form an inhibitor capable of blocking formation~~ of the ~~polar Z ring septums. Rapidly oscillates between~~ the ~~poles~~ of the ~~cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings~~.~~<ref>~~PMID:~~1836760</ref>~~ <ref>PMID:~~22380631~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3q9l]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021231967</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Holyoak, T.]]	+	[[Category: Holyoak, T]]
-	[[Category: Lutkenhaus, J.]]	+	[[Category: Lutkenhaus, J]]
-	[[Category: Park, K T.]]	+	[[Category: Park, K T]]
-	[[Category: Wu, W.]]	+	[[Category: Wu, W]]
	[[Category: Atpase]]		[[Category: Atpase]]
	[[Category: Bacterial cell division inhibitor]]		[[Category: Bacterial cell division inhibitor]]

OCA at 08:31, 8 May 2013

OCA — Wed, 08 May 2013 08:31:42 GMT

←Older revision		Revision as of 08:31, 8 May 2013
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-	[[Image:3q9l.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3q9l", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
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	{{STRUCTURE_3q9l\| PDB=3q9l \| SCENE= }}		{{STRUCTURE_3q9l\| PDB=3q9l \| SCENE= }}
-
	===The structure of the dimeric E.coli MinD-ATP complex===		===The structure of the dimeric E.coli MinD-ATP complex===
		+	{{ABSTRACT_PUBMED_21231967}}

-		+	==Function==
-	~~<!--~~	+	[[http://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI]] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21231967}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov), where 21231967 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_21231967}}~~	+

	==About this Structure==		==About this Structure==
Line 22:		Line 10:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~21231967~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021231967</ref><references group="xtra"/><references/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Holyoak, T.]]		[[Category: Holyoak, T.]]
Line 28:		Line 16:
	[[Category: Park, K T.]]		[[Category: Park, K T.]]
	[[Category: Wu, W.]]		[[Category: Wu, W.]]
		+	[[Category: Atpase]]
		+	[[Category: Bacterial cell division inhibitor]]
		+	[[Category: Cell cycle]]
		+	[[Category: Hydrolase]]
		+	[[Category: Minc]]
		+	[[Category: Mine]]

OCA at 06:25, 23 March 2011

OCA — Wed, 23 Mar 2011 06:25:37 GMT

←Older revision		Revision as of 06:25, 23 March 2011
Line 1:		Line 1:
-	[[Image:3q9l.~~jpg~~\|left\|200px]]	+	[[Image:3q9l.png\|left\|200px]]

	<!--		<!--

OCA at 13:06, 26 January 2011

OCA — Wed, 26 Jan 2011 13:06:41 GMT

←Older revision		Revision as of 13:06, 26 January 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3q9l.jpg\|left\|200px]]

-	The ~~entry 3q9l~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3q9l", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3q9l\| PDB=3q9l \| SCENE= }}

-	~~Authors: Wu, W., Park, K~~.-~~T., Lutkenhaus, J., Holyoak, T.~~	+	===The structure of the dimeric E.coli MinD-ATP complex===

-	~~Description:~~ The ~~structure of~~ the ~~dimeric E~~.coli ~~MinD~~-~~ATP complex~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21231967}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21231967 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21231967}}
		+
		+	==About this Structure==
		+	[[3q9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9L OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:21231967</ref><references group="xtra"/>
		+	[[Category: Escherichia coli]]
		+	[[Category: Holyoak, T.]]
		+	[[Category: Lutkenhaus, J.]]
		+	[[Category: Park, K T.]]
		+	[[Category: Wu, W.]]

OCA: Protected "3q9l" [edit=sysop:move=sysop]

OCA — Wed, 19 Jan 2011 05:51:53 GMT

Protected "3q9l" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:51, 19 January 2011

OCA: New page: '''Unreleased structure''' The entry 3q9l is ON HOLD Authors: Wu, W., Park, K.-T., Lutkenhaus, J., Holyoak, T. Description: The structure of the dimeric E.coli MinD-ATP complex

OCA — Wed, 19 Jan 2011 05:51:53 GMT

New page: '''Unreleased structure''' The entry 3q9l is ON HOLD Authors: Wu, W., Park, K.-T., Lutkenhaus, J., Holyoak, T. Description: The structure of the dimeric E.coli MinD-ATP complex

New page

'''Unreleased structure'''

The entry 3q9l is ON HOLD

Authors: Wu, W., Park, K.-T., Lutkenhaus, J., Holyoak, T.

Description: The structure of the dimeric E.coli MinD-ATP complex