1f7x - Revision history

OCA at 08:28, 22 May 2024

OCA — Wed, 22 May 2024 08:28:09 GMT

←Older revision		Revision as of 08:28, 22 May 2024
Line 19:		Line 19:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f7x ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f7x ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	ZipA, an essential component of cell division in Escherichia coli, interacts with the FtsZ protein at the midcell in one of the initial steps of septum formation. The high-resolution solution structure of the 144-residue C-terminal domain of E. coli ZipA (ZipA(185)(-)(328)) has been determined by multidimensional heteronuclear NMR. A total of 30 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 2758 experimental NMR restraints. The atomic root means square distribution about the mean coordinate positions for residues 6-142 for the 30 structures is 0.37 +/- 0.04 A for the backbone atoms, 0. 78 +/- 0.05 A for all atoms, and 0.45 +/- 0.04 A for all atoms excluding disordered side chains. The NMR solution structure of ZipA(185)(-)(328) is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands where the alpha-helices and the beta-sheet form surfaces directly opposite each other. A C-terminal peptide from FtsZ has been shown to bind ZipA(185)(-)(328) in a hydrophobic channel formed by the beta-sheet providing insight into the ZipA-FtsZ interaction. An unexpected similarity between the ZipA(185)(-)(328) fold and the split beta-alpha-beta fold observed in many RNA binding proteins may further our understanding of the critical ZipA-FtsZ interaction.
		+
		+	Solution structure of ZipA, a crucial component of Escherichia coli cell division.,Moy FJ, Glasfeld E, Mosyak L, Powers R Biochemistry. 2000 Aug 8;39(31):9146-56. PMID:10924108<ref>PMID:10924108</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1f7x" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cell division protein 3D structures\|Cell division protein 3D structures]]		*[[Cell division protein 3D structures\|Cell division protein 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:11, 20 March 2024

OCA — Wed, 20 Mar 2024 10:11:22 GMT

←Older revision		Revision as of 10:11, 20 March 2024
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==		==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==
-	<StructureSection load='1f7x' size='340' side='right'caption='[[1f7x~~]], [[NMR_Ensembles_of_Models \| 30 NMR models~~]]' scene=''>	+	<StructureSection load='1f7x' size='340' side='right'caption='[[1f7x]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F7X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[1f7w\|1f7w]]</div~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [https://pdbe.org/1f7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [https://www.ebi.ac.uk/pdbsum/1f7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7x 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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [https://pdbe.org/1f7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [https://www.ebi.ac.uk/pdbsum/1f7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ZIPA_ECOLI ZIPA_ECOLI]] Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509]	+	[https://www.uniprot.org/uniprot/ZIPA_ECOLI ZIPA_ECOLI] Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 19:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f7x ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f7x ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	ZipA, an essential component of cell division in Escherichia coli, interacts with the FtsZ protein at the midcell in one of the initial steps of septum formation. The high-resolution solution structure of the 144-residue C-terminal domain of E. coli ZipA (ZipA(185)(-)(328)) has been determined by multidimensional heteronuclear NMR. A total of 30 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 2758 experimental NMR restraints. The atomic root means square distribution about the mean coordinate positions for residues 6-142 for the 30 structures is 0.37 +/- 0.04 A for the backbone atoms, 0. 78 +/- 0.05 A for all atoms, and 0.45 +/- 0.04 A for all atoms excluding disordered side chains. The NMR solution structure of ZipA(185)(-)(328) is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands where the alpha-helices and the beta-sheet form surfaces directly opposite each other. A C-terminal peptide from FtsZ has been shown to bind ZipA(185)(-)(328) in a hydrophobic channel formed by the beta-sheet providing insight into the ZipA-FtsZ interaction. An unexpected similarity between the ZipA(185)(-)(328) fold and the split beta-alpha-beta fold observed in many RNA binding proteins may further our understanding of the critical ZipA-FtsZ interaction.
-
-	Solution structure of ZipA, a crucial component of Escherichia coli cell division.,Moy FJ, Glasfeld E, Mosyak L, Powers R Biochemistry. 2000 Aug 8;39(31):9146-56. PMID:10924108<ref>PMID:10924108</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1f7x" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cell division protein 3D structures\|Cell division protein 3D structures]]		*[[Cell division protein 3D structures\|Cell division protein 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Glasfeld, E]]	+	[[Category: Glasfeld E]]
-	[[Category: Mosyak, L]]	+	[[Category: Mosyak L]]
-	[[Category: Moy~~, F J~~]]	+	[[Category: Moy FJ]]
-	[[Category: Powers, R]]	+	[[Category: Powers R]]
-	~~[[Category: Alpha-beta fold]]~~	+
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Cell division]]~~	+
-	~~[[Category: Inner membrane]]~~	+
-	~~[[Category: Septation]]~~	+
-	~~[[Category: Transmembrane~~]]	+

OCA at 09:47, 21 July 2021

OCA — Wed, 21 Jul 2021 09:47:25 GMT

←Older revision		Revision as of 09:47, 21 July 2021
Line 3:		Line 3:
	<StructureSection load='1f7x' size='340' side='right'caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='1f7x' size='340' side='right'caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1F7X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f7w\|1f7w]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f7w\|1f7w]]</div></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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [~~http~~://pdbe.org/1f7x PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1f7x PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7x 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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [https://pdbe.org/1f7x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [https://www.ebi.ac.uk/pdbsum/1f7x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ZIPA_ECOLI ZIPA_ECOLI]] Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509]	+	[[https://www.uniprot.org/uniprot/ZIPA_ECOLI ZIPA_ECOLI]] Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:29, 16 October 2019

OCA — Wed, 16 Oct 2019 10:29:55 GMT

←Older revision		Revision as of 10:29, 16 October 2019
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==		==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==
-	<StructureSection load='1f7x' size='340' side='right' caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>	+	<StructureSection load='1f7x' size='340' side='right'caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>		<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1f7x" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1f7x" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cell division protein 3D structures\|Cell division protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 33:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus coli migula 1895]]		[[Category: Bacillus coli migula 1895]]
		+	[[Category: Large Structures]]
	[[Category: Glasfeld, E]]		[[Category: Glasfeld, E]]
	[[Category: Mosyak, L]]		[[Category: Mosyak, L]]

OCA at 09:27, 27 December 2017

OCA — Wed, 27 Dec 2017 09:27:18 GMT

←Older revision		Revision as of 09:27, 27 December 2017
Line 1:		Line 1:
		+
	==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==		==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==
	<StructureSection load='1f7x' size='340' side='right' caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='1f7x' size='340' side='right' caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>		<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f7w\|1f7w]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f7w\|1f7w]]</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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://pdbe.org/1f7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x 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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://pdbe.org/1f7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f7x ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/1f7x_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/1f7x_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 09:09, 8 February 2016

OCA — Mon, 08 Feb 2016 09:09:15 GMT

←Older revision		Revision as of 09:09, 8 February 2016
Line 16:		Line 16:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f7x ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 10:03, 10 September 2015

OCA — Thu, 10 Sep 2015 10:03:16 GMT

←Older revision		Revision as of 10:03, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1f7x' size='340' side='right' caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='1f7x' size='340' side='right' caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia~~ coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f7w\|1f7w]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f7w\|1f7w]]</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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x 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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://pdbe.org/1f7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1f7x" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia~~ coli]]	+	[[Category: Bacillus coli migula 1895]]
	[[Category: Glasfeld, E]]		[[Category: Glasfeld, E]]
	[[Category: Mosyak, L]]		[[Category: Mosyak, L]]

OCA at 22:11, 24 December 2014

OCA — Wed, 24 Dec 2014 22:11:49 GMT

←Older revision		Revision as of 22:11, 24 December 2014
Line 6:		Line 6:
	<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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x 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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ZIPA_ECOLI ZIPA_ECOLI]] Interacts directly with the cell division protein FtsZ. Probable receptor for the septal ring structure, may anchor it to the inner-membrane.[HAMAP-Rule:MF_00509]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 18:24, 22 December 2014

OCA — Mon, 22 Dec 2014 18:24:57 GMT

←Older revision		Revision as of 18:24, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>		<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f7w\|1f7w]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f7w\|1f7w]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x 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=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Glasfeld, E.]]	+	[[Category: Glasfeld, E]]
-	[[Category: Mosyak, L.]]	+	[[Category: Mosyak, L]]
-	[[Category: Moy, F J.]]	+	[[Category: Moy, F J]]
-	[[Category: Powers, R.]]	+	[[Category: Powers, R]]
	[[Category: Alpha-beta fold]]		[[Category: Alpha-beta fold]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]

OCA at 08:28, 28 September 2014

OCA — Sun, 28 Sep 2014 08:28:50 GMT

←Older revision		Revision as of 08:28, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1f7x.~~png~~\|~~left~~\|200px]]	+	==SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA==
		+	<StructureSection load='1f7x' size='340' side='right' caption='[[1f7x]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1f7x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F7X FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f7w\|1f7w]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f7x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f7x RCSB], [http://www.ebi.ac.uk/pdbsum/1f7x PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/1f7x_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	ZipA, an essential component of cell division in Escherichia coli, interacts with the FtsZ protein at the midcell in one of the initial steps of septum formation. The high-resolution solution structure of the 144-residue C-terminal domain of E. coli ZipA (ZipA(185)(-)(328)) has been determined by multidimensional heteronuclear NMR. A total of 30 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 2758 experimental NMR restraints. The atomic root means square distribution about the mean coordinate positions for residues 6-142 for the 30 structures is 0.37 +/- 0.04 A for the backbone atoms, 0. 78 +/- 0.05 A for all atoms, and 0.45 +/- 0.04 A for all atoms excluding disordered side chains. The NMR solution structure of ZipA(185)(-)(328) is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands where the alpha-helices and the beta-sheet form surfaces directly opposite each other. A C-terminal peptide from FtsZ has been shown to bind ZipA(185)(-)(328) in a hydrophobic channel formed by the beta-sheet providing insight into the ZipA-FtsZ interaction. An unexpected similarity between the ZipA(185)(-)(328) fold and the split beta-alpha-beta fold observed in many RNA binding proteins may further our understanding of the critical ZipA-FtsZ interaction.

-	~~{{STRUCTURE_1f7x\| PDB=1f7x \| SCENE= }}~~	+	Solution structure of ZipA, a crucial component of Escherichia coli cell division.,Moy FJ, Glasfeld E, Mosyak L, Powers R Biochemistry. 2000 Aug 8;39(31):9146-56. PMID:10924108<ref>PMID:10924108</ref>

-	~~===SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~==About this Structure==~~	+	<references/>
-	~~[[1f7x]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1F7X OCA].~~	+	__TOC__
-		+	</StructureSection>
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:010924108<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Glasfeld, E.]]		[[Category: Glasfeld, E.]]