1j2a - Revision history

OCA at 07:14, 25 October 2023

2023-10-25T07:14:23Z

←Older revision		Revision as of 07:14, 25 October 2023
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	<StructureSection load='1j2a' size='340' side='right'caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1j2a' size='340' side='right'caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1j2a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J2A FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1j2a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J2A 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;'>[[1j28\|1j28]]~~, [[~~1j29~~\|~~1j29~~]]~~</div></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]] 1.8Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 ~~5.2.1.8] </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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [https://pdbe.org/1j2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [https://www.ebi.ac.uk/pdbsum/1j2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2a 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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [https://pdbe.org/1j2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [https://www.ebi.ac.uk/pdbsum/1j2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2a ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PPIA_ECOLI PPIA_ECOLI]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:2190212</ref>	+	[https://www.uniprot.org/uniprot/PPIA_ECOLI PPIA_ECOLI] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:2190212</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Peptidylprolyl isomerase]]~~	+	[[Category: Fushinobu S]]
-	[[Category: Fushinobu, S]]	+	[[Category: Kawaguchi Y]]
-	[[Category: Kawaguchi, Y]]	+	[[Category: Konno M]]
-	[[Category: Konno, M]]	+	[[Category: Matsuzawa H]]
-	[[Category: Matsuzawa, H]]	+	[[Category: Okudaira K]]
-	[[Category: Okudaira, K]]	+	[[Category: Sano Y]]
-	[[Category: Sano, Y]]	+	[[Category: Yamagishi-Ohmori Y]]
-	[[Category: Yamagishi-Ohmori, Y]]	+
-	~~[[Category: Beta barrel]]~~	+
-	~~[[Category: Isomerase~~]]	+

OCA at 11:09, 4 August 2021

2021-08-04T11:09:38Z

←Older revision		Revision as of 11:09, 4 August 2021
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	<StructureSection load='1j2a' size='340' side='right'caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1j2a' size='340' side='right'caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1j2a]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2A OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1J2A FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1j2a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J2A FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j28\|1j28]], [[1j29\|1j29]]</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;'>[[1j28\|1j28]], [[1j29\|1j29]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [~~http~~://pdbe.org/1j2a PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1j2a PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2a 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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [https://pdbe.org/1j2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [https://www.ebi.ac.uk/pdbsum/1j2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2a ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PPIA_ECOLI PPIA_ECOLI]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:2190212</ref>	+	[[https://www.uniprot.org/uniprot/PPIA_ECOLI PPIA_ECOLI]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:2190212</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:18, 30 October 2019

2019-10-30T10:18:59Z

←Older revision		Revision as of 10:18, 30 October 2019
Line 1:		Line 1:

	==Structure of E. coli cyclophilin B K163T mutant==		==Structure of E. coli cyclophilin B K163T mutant==
-	<StructureSection load='1j2a' size='340' side='right' caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='1j2a' size='340' side='right'caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1j2a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J2A FirstGlance]. <br>		<table><tr><td colspan='2'>[[1j2a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J2A FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 1j2a" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1j2a" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Bacillus coli migula 1895]]		[[Category: Bacillus coli migula 1895]]
		+	[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Fushinobu, S]]		[[Category: Fushinobu, S]]

OCA at 09:04, 17 January 2018

2018-01-17T09:04:00Z

←Older revision		Revision as of 09:04, 17 January 2018
Line 1:		Line 1:
		+
	==Structure of E. coli cyclophilin B K163T mutant==		==Structure of E. coli cyclophilin B K163T mutant==
	<StructureSection load='1j2a' size='340' side='right' caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1j2a' size='340' side='right' caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j28\|1j28]], [[1j29\|1j29]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j28\|1j28]], [[1j29\|1j29]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [http://pdbe.org/1j2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [http://www.ebi.ac.uk/pdbsum/1j2a 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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [http://pdbe.org/1j2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [http://www.ebi.ac.uk/pdbsum/1j2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2a ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j2/1j2a_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j2/1j2a_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>
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1j2a" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1j2a" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cyclophilin\|Cyclophilin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 03:00, 7 February 2016

2016-02-07T03:00:12Z

←Older revision		Revision as of 03:00, 7 February 2016
Line 17:		Line 17:
	<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=1j2a ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:01, 9 September 2015

2015-09-09T21:01:57Z

←Older revision		Revision as of 21:01, 9 September 2015
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	<StructureSection load='1j2a' size='340' side='right' caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1j2a' size='340' side='right' caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1j2a]] is a 1 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=1J2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J2A FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1j2a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J2A FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j28\|1j28]], [[1j29\|1j29]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j28\|1j28]], [[1j29\|1j29]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [http://www.ebi.ac.uk/pdbsum/1j2a 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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [http://pdbe.org/1j2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [http://www.ebi.ac.uk/pdbsum/1j2a PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 1j2a" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia~~ coli]]	+	[[Category: Bacillus coli migula 1895]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Fushinobu, S]]		[[Category: Fushinobu, S]]

OCA at 07:19, 24 December 2014

2014-12-24T07:19:14Z

←Older revision		Revision as of 07:19, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1j2a]] is a 1 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=1J2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J2A FirstGlance]. <br>		<table><tr><td colspan='2'>[[1j2a]] is a 1 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=1J2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J2A FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j28\|1j28]], [[1j29\|1j29]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j28\|1j28]], [[1j29\|1j29]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [http://www.ebi.ac.uk/pdbsum/1j2a 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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [http://www.ebi.ac.uk/pdbsum/1j2a PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PPIA_ECOLI PPIA_ECOLI]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:2190212</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
-	[[Category: Fushinobu, S.]]	+	[[Category: Fushinobu, S]]
-	[[Category: Kawaguchi, Y.]]	+	[[Category: Kawaguchi, Y]]
-	[[Category: Konno, M.]]	+	[[Category: Konno, M]]
-	[[Category: Matsuzawa, H.]]	+	[[Category: Matsuzawa, H]]
-	[[Category: Okudaira, K.]]	+	[[Category: Okudaira, K]]
-	[[Category: Sano, Y.]]	+	[[Category: Sano, Y]]
-	[[Category: Yamagishi-Ohmori, Y.]]	+	[[Category: Yamagishi-Ohmori, Y]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]
	[[Category: Isomerase]]		[[Category: Isomerase]]

OCA at 08:48, 28 September 2014

2014-09-28T08:48:12Z

←Older revision		Revision as of 08:48, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1j2a.~~png~~\|~~left~~\|200px]]	+	==Structure of E. coli cyclophilin B K163T mutant==
		+	<StructureSection load='1j2a' size='340' side='right' caption='[[1j2a]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1j2a]] is a 1 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=1J2A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J2A FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1j28\|1j28]], [[1j29\|1j29]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></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=1j2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j2a RCSB], [http://www.ebi.ac.uk/pdbsum/1j2a 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/j2/1j2a_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 ==
		+	Cyclophilins facilitate the peptidyl-prolyl isomerization of a trans-isomer to a cis-isomer in the refolding process of unfolded proteins to recover the natural folding state with cis-proline conformation. To date, only short peptides with a cis-form proline have been observed in complexes of human and Escherichia coli proteins of cyclophilin A, which is present in cytoplasm. The crystal structures analyzed in this study show two complexes in which peptides having a trans-form proline, i.e. succinyl-Ala-trans-Pro-Ala-p-nitroanilide and acetyl-Ala-Ala-trans-Pro-Ala-amidomethylcoumarin, are bound on a K163T mutant of Escherichia coli cyclophilin B, the preprotein of which has a signal sequence. Comparison with cis-form peptides bound to cyclophilin A reveals that in any case the proline ring is inserted into the hydrophobic pocket and a hydrogen bond between CO of Pro and Neta2 of Arg is formed to fix the peptide. On the other hand, in the cis-isomer, the formation of two hydrogen bonds of NH and CO of Ala preceding Pro with the protein fixes the peptide, whereas in the trans-isomer formation of a hydrogen bond between CO preceding Ala-Pro and His47 Nepsilon2 via a mediating water molecule allows the large distortion in the orientation of Ala of Ala-Pro. Although loss of double bond character of the amide bond of Ala-Pro is essential to the isomerization pathway occurring by rotating around its bond, these peptides have forms impossible to undergo proton transfer from the guanidyl group of Arg to the prolyl N atom, which induces loss of double bond character.

-	~~{{STRUCTURE_1j2a\| PDB=1j2a \| SCENE= }}~~	+	Escherichia coli cyclophilin B binds a highly distorted form of trans-prolyl peptide isomer.,Konno M, Sano Y, Okudaira K, Kawaguchi Y, Yamagishi-Ohmori Y, Fushinobu S, Matsuzawa H Eur J Biochem. 2004 Sep;271(18):3794-803. PMID:15355356<ref>PMID:15355356</ref>

-	~~===Structure~~ of E. ~~coli cyclophilin B K163T mutant===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15355356}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1j2a]] is a 1 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=1J2A OCA].~~	+

	==See Also==		==See Also==
	*[[Cyclophilin\|Cyclophilin]]		*[[Cyclophilin\|Cyclophilin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:015355356<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]

OCA at 05:24, 20 October 2012

2012-10-20T05:24:45Z

←Older revision		Revision as of 05:24, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1j2a]] is a 1 chain structure ~~of [[Cyclophilin]]~~ 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=1J2A OCA].	+	[[1j2a]] is a 1 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=1J2A OCA].

	==See Also==		==See Also==

OCA at 09:57, 25 July 2012

2012-07-25T09:57:07Z

←Older revision		Revision as of 09:57, 25 July 2012
Line 1:		Line 1:
	[[Image:1j2a.png\|left\|200px]]		[[Image:1j2a.png\|left\|200px]]

-	<!--
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-	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_1j2a\| PDB=1j2a \| SCENE= }}		{{STRUCTURE_1j2a\| PDB=1j2a \| SCENE= }}

	===Structure of E. coli cyclophilin B K163T mutant===		===Structure of E. coli cyclophilin B K163T mutant===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15355356}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15355356 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_15355356}}		{{ABSTRACT_PUBMED_15355356}}

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	==See Also==		==See Also==
-	*[[Cyclophilin]]	+	*[[Cyclophilin\|Cyclophilin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15355356~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015355356</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]