1prr - Revision history

OCA at 09:00, 22 May 2024

OCA — Wed, 22 May 2024 09:00:25 GMT

←Older revision		Revision as of 09:00, 22 May 2024
Line 20:		Line 20:
	</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=1prr 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=1prr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is evolutionarily related to vertebrate lens beta gamma-crystallins. RESULTS: The three-dimensional solution structure of Ca(2+)-loaded protein S has been determined using multi-dimensional heteronuclear NMR spectroscopy. (Sixty structures were calculated, from which thirty were selected with a root mean square difference from the mean of 0.38 A for backbone atoms and 1.22 A for all non-hydrogen atoms.) The structure was analyzed and compared in detail with X-ray crystallographic structures of beta gamma-crystallins. The two internally homologous domains of protein S were compared, and hydrophobic cores, domain interfaces, surface ion pairing, amino-aromatic interactions and potential modes of multimerization are discussed. CONCLUSIONS: Structural features of protein S described here help to explain its overall thermostability, as well as the higher stability and Ca2+ affinity of the amino-terminal domain relative to the carboxy-terminal domain. Two potential modes of multimerization are proposed involving cross-linking of protein S molecules through surface Ca(2+)-binding sites and formation of the intramolecular protein S or gamma B-crystallin interdomain interface in an intermolecular content. This structural analysis may also have implications for Ca(2+)-dependent cell-cell interactions mediated by the vertebrate cadherins and Dictyostelium discoideum protein gp24.
		+
		+	NMR-derived three-dimensional solution structure of protein S complexed with calcium.,Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M Structure. 1994 Feb 15;2(2):107-22. PMID:8081742<ref>PMID:8081742</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1prr" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 05:58, 17 April 2024

OCA — Wed, 17 Apr 2024 05:58:24 GMT

←Older revision		Revision as of 05:58, 17 April 2024
Line 1:		Line 1:

	==NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM==		==NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM==
-	<StructureSection load='1prr' size='340' side='right'caption='[[1prr~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1prr' size='340' side='right'caption='[[1prr]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_25232 Atcc 25232~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRR FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~</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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1prs\|1prs]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [https://pdbe.org/1prr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [https://www.ebi.ac.uk/pdbsum/1prr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prr 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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [https://pdbe.org/1prr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [https://www.ebi.ac.uk/pdbsum/1prr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DESS_MYXXA DESS_MYXXA]] Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.	+	[https://www.uniprot.org/uniprot/DESS_MYXXA DESS_MYXXA] Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</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=1prr 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=1prr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is evolutionarily related to vertebrate lens beta gamma-crystallins. RESULTS: The three-dimensional solution structure of Ca(2+)-loaded protein S has been determined using multi-dimensional heteronuclear NMR spectroscopy. (Sixty structures were calculated, from which thirty were selected with a root mean square difference from the mean of 0.38 A for backbone atoms and 1.22 A for all non-hydrogen atoms.) The structure was analyzed and compared in detail with X-ray crystallographic structures of beta gamma-crystallins. The two internally homologous domains of protein S were compared, and hydrophobic cores, domain interfaces, surface ion pairing, amino-aromatic interactions and potential modes of multimerization are discussed. CONCLUSIONS: Structural features of protein S described here help to explain its overall thermostability, as well as the higher stability and Ca2+ affinity of the amino-terminal domain relative to the carboxy-terminal domain. Two potential modes of multimerization are proposed involving cross-linking of protein S molecules through surface Ca(2+)-binding sites and formation of the intramolecular protein S or gamma B-crystallin interdomain interface in an intermolecular content. This structural analysis may also have implications for Ca(2+)-dependent cell-cell interactions mediated by the vertebrate cadherins and Dictyostelium discoideum protein gp24.
-
-	NMR-derived three-dimensional solution structure of protein S complexed with calcium.,Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M Structure. 1994 Feb 15;2(2):107-22. PMID:8081742<ref>PMID:8081742</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1prr" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 25232]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bagby, S]]	+	[[Category: Myxococcus xanthus]]
-	[[Category: Eagle~~, S G~~]]	+	[[Category: Bagby S]]
-	[[Category: Harvey~~, T S~~]]	+	[[Category: Eagle SG]]
-	[[Category: Ikura, M]]	+	[[Category: Harvey TS]]
-	[[Category: Inouye, S]]	+	[[Category: Ikura M]]
-	~~[[Category: Binding protein~~]]	+	[[Category: Inouye S]]

OCA at 09:33, 8 September 2021

OCA — Wed, 08 Sep 2021 09:33:50 GMT

←Older revision		Revision as of 09:33, 8 September 2021
Line 3:		Line 3:
	<StructureSection load='1prr' size='340' side='right'caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1prr' size='340' side='right'caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1PRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1prs\|1prs]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1prs\|1prs]]</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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [~~http~~://pdbe.org/1prr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1prr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1prr 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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [https://pdbe.org/1prr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [https://www.ebi.ac.uk/pdbsum/1prr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DESS_MYXXA DESS_MYXXA]] Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.	+	[[https://www.uniprot.org/uniprot/DESS_MYXXA DESS_MYXXA]] Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:50, 27 November 2019

OCA — Wed, 27 Nov 2019 09:50:49 GMT

←Older revision		Revision as of 09:50, 27 November 2019
Line 1:		Line 1:

	==NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM==		==NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM==
-	<StructureSection load='1prr' size='340' side='right' caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1prr' size='340' side='right'caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRR FirstGlance]. <br>		<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRR FirstGlance]. <br>
Line 34:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 25232]]		[[Category: Atcc 25232]]
		+	[[Category: Large Structures]]
	[[Category: Bagby, S]]		[[Category: Bagby, S]]
	[[Category: Eagle, S G]]		[[Category: Eagle, S G]]

OCA at 07:56, 24 February 2018

OCA — Sat, 24 Feb 2018 07:56:53 GMT

←Older revision		Revision as of 07:56, 24 February 2018
Line 1:		Line 1:
		+
	==NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM==		==NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM==
	<StructureSection load='1prr' size='340' side='right' caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1prr' size='340' side='right' caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1prs\|1prs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1prs\|1prs]]</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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [http://pdbe.org/1prr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [http://www.ebi.ac.uk/pdbsum/1prr 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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [http://pdbe.org/1prr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [http://www.ebi.ac.uk/pdbsum/1prr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1prr ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1prr_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1prr_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>
	</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=1prr ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 08:17, 11 September 2015

OCA — Fri, 11 Sep 2015 08:17:04 GMT

←Older revision		Revision as of 08:17, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1prr' size='340' side='right' caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1prr' size='340' side='right' caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Myxococcus_xanthus Myxococcus xanthus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1prs\|1prs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1prs\|1prs]]</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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [http://www.ebi.ac.uk/pdbsum/1prr 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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [http://pdbe.org/1prr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [http://www.ebi.ac.uk/pdbsum/1prr PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1prr" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Myxococcus xanthus~~]]	+	[[Category: Atcc 25232]]
	[[Category: Bagby, S]]		[[Category: Bagby, S]]
	[[Category: Eagle, S G]]		[[Category: Eagle, S G]]

OCA at 13:44, 25 December 2014

OCA — Thu, 25 Dec 2014 13:44:48 GMT

←Older revision		Revision as of 13:44, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRR FirstGlance]. <br>		<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRR FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1prs\|1prs]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1prs\|1prs]]</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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [http://www.ebi.ac.uk/pdbsum/1prr 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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [http://www.ebi.ac.uk/pdbsum/1prr PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DESS_MYXXA DESS_MYXXA]] Protein S, induced in large amounts during fruiting body formation, assembles on the surface of myxospores in the presence of calcium ions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Myxococcus xanthus]]		[[Category: Myxococcus xanthus]]
-	[[Category: Bagby, S.]]	+	[[Category: Bagby, S]]
-	[[Category: Eagle, S G.]]	+	[[Category: Eagle, S G]]
-	[[Category: Harvey, T S.]]	+	[[Category: Harvey, T S]]
-	[[Category: Ikura, M.]]	+	[[Category: Ikura, M]]
-	[[Category: Inouye, S.]]	+	[[Category: Inouye, S]]
	[[Category: Binding protein]]		[[Category: Binding protein]]

OCA at 22:43, 28 September 2014

OCA — Sun, 28 Sep 2014 22:43:40 GMT

←Older revision		Revision as of 22:43, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1prr.~~png~~\|~~left~~\|200px]]	+	==NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM==
		+	<StructureSection load='1prr' size='340' side='right' caption='[[1prr]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1prr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRR FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1prs\|1prs]]</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=1prr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1prr RCSB], [http://www.ebi.ac.uk/pdbsum/1prr 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/pr/1prr_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 ==
		+	BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is evolutionarily related to vertebrate lens beta gamma-crystallins. RESULTS: The three-dimensional solution structure of Ca(2+)-loaded protein S has been determined using multi-dimensional heteronuclear NMR spectroscopy. (Sixty structures were calculated, from which thirty were selected with a root mean square difference from the mean of 0.38 A for backbone atoms and 1.22 A for all non-hydrogen atoms.) The structure was analyzed and compared in detail with X-ray crystallographic structures of beta gamma-crystallins. The two internally homologous domains of protein S were compared, and hydrophobic cores, domain interfaces, surface ion pairing, amino-aromatic interactions and potential modes of multimerization are discussed. CONCLUSIONS: Structural features of protein S described here help to explain its overall thermostability, as well as the higher stability and Ca2+ affinity of the amino-terminal domain relative to the carboxy-terminal domain. Two potential modes of multimerization are proposed involving cross-linking of protein S molecules through surface Ca(2+)-binding sites and formation of the intramolecular protein S or gamma B-crystallin interdomain interface in an intermolecular content. This structural analysis may also have implications for Ca(2+)-dependent cell-cell interactions mediated by the vertebrate cadherins and Dictyostelium discoideum protein gp24.

-	~~{{STRUCTURE_1prr\| PDB=1prr \| SCENE= }}~~	+	NMR-derived three-dimensional solution structure of protein S complexed with calcium.,Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M Structure. 1994 Feb 15;2(2):107-22. PMID:8081742<ref>PMID:8081742</ref>

-	~~===NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8081742}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1prr]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Myxococcus_xanthus Myxococcus xanthus]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:008081742<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Myxococcus xanthus]]		[[Category: Myxococcus xanthus]]
	[[Category: Bagby, S.]]		[[Category: Bagby, S.]]

OCA: Protected "1prr" [edit=sysop:move=sysop]

OCA — Wed, 19 Dec 2012 11:53:36 GMT

Protected "1prr" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:53, 19 December 2012

OCA at 11:53, 19 December 2012

OCA — Wed, 19 Dec 2012 11:53:32 GMT

←Older revision		Revision as of 11:53, 19 December 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1prr.png\|left\|200px]]		[[Image:1prr.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1prr", 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_1prr\| PDB=1prr \| SCENE= }}		{{STRUCTURE_1prr\| PDB=1prr \| SCENE= }}

	===NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM===		===NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S COMPLEXED WITH CALCIUM===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_8081742}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 8081742 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_8081742}}		{{ABSTRACT_PUBMED_8081742}}

	==About this Structure==		==About this Structure==
-	~~1PRR~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA].	+	[[1prr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRR OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~8081742~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008081742</ref><references group="xtra"/>
	[[Category: Myxococcus xanthus]]		[[Category: Myxococcus xanthus]]
	[[Category: Bagby, S.]]		[[Category: Bagby, S.]]
Line 31:		Line 19:
	[[Category: Inouye, S.]]		[[Category: Inouye, S.]]
	[[Category: Binding protein]]		[[Category: Binding protein]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:46:49 2009''