2req - Revision history

OCA at 08:36, 13 August 2026

2026-08-13T08:36:18Z

← Older revision		Revision as of 08:36, 13 August 2026
Line 5:		Line 5:
	<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2REQ FirstGlance]. <br>
	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.5Å</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]] 2.5Å</td></tr>
	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat">~~<scene name='pdbligand=B12:COBALAMIN'>B12</scene>,~~ <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [https://pdbe.org/2req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [https://www.ebi.ac.uk/pdbsum/2req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2req 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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [https://pdbe.org/2req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [https://www.ebi.ac.uk/pdbsum/2req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2req ProSAT]</span></td></tr>
	</table>		</table>
Line 15:		Line 15:
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/2req_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/2req_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 06:46, 9 August 2023

2023-08-09T06:46:41Z

← Older revision		Revision as of 06:46, 9 August 2023
Line 3:		Line 3:
	<StructureSection load='2req' size='340' side='right'caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2req' size='340' side='right'caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"propionibacterium_shermanii"_van_niel_1928 "propionibacterium~~ shermanii~~" van niel 1928~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2REQ FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=B12:COBALAMIN'>B12</scene>~~, ~~<scene name='pdbligand=COA:COENZYME+A'>COA</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]] 2.5Å</td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>MUTA, MUTB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1752~~ "~~Propionibacterium shermanii~~" ~~van Niel 1928])</td~~><~~/tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2]~~ </~~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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [https://pdbe.org/2req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [https://www.ebi.ac.uk/pdbsum/2req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2req 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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [https://pdbe.org/2req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [https://www.ebi.ac.uk/pdbsum/2req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2req ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR~~]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. [[https://www.uniprot.org/uniprot/MUTA_PROFR MUTA_PROFR]~~] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.		[https://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Propionibacterium shermanii van niel 1928]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Methylmalonyl-CoA mutase~~]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
	[[Category: Evans~~, P R~~]]		[[Category: Evans PR]]
	[[Category: Mancia, F]]		[[Category: Mancia F]]
	~~[[Category: Intramolecular transferase]]~~
	~~[[Category: Isomerase]]~~
	~~[[Category: Mutase~~]]

OCA at 04:23, 2 July 2021

2021-07-02T04:23:10Z

← Older revision		Revision as of 04:23, 2 July 2021
Line 1:		Line 1:

	==METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE==		==METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE==
	<StructureSection load='2req' size='340' side='right' caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2req' size='340' side='right'caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2REQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [~~http~~://pdbe.org/2req PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2req PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2req 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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [https://pdbe.org/2req PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [https://www.ebi.ac.uk/pdbsum/2req PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2req ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. [[~~http~~://www.uniprot.org/uniprot/MUTA_PROFR MUTA_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.		[[https://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. [[https://www.uniprot.org/uniprot/MUTA_PROFR MUTA_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Propionibacterium shermanii van niel 1928]]		[[Category: Propionibacterium shermanii van niel 1928]]
			[[Category: Large Structures]]
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Evans, P R]]		[[Category: Evans, P R]]

OCA at 11:35, 5 September 2018

2018-09-05T11:35:54Z

← Older revision		Revision as of 11:35, 5 September 2018
Line 1:		Line 1:

	==METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE==		==METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE==
	<StructureSection load='2req' size='340' side='right' caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2req' size='340' side='right' caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [http://pdbe.org/2req PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [http://www.ebi.ac.uk/pdbsum/2req 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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [http://pdbe.org/2req PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [http://www.ebi.ac.uk/pdbsum/2req PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2req ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/2req_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/2req_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 02:01, 9 February 2016

2016-02-09T02:01:33Z

← Older revision		Revision as of 02:01, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='2req' size='340' side='right' caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2req' size='340' side='right' caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp.~~ shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2REQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium ~~freudenreichii subsp.~~ shermanii])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 "Propionibacterium shermanii" van Niel 1928])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [http://www.ebi.ac.uk/pdbsum/2req 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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [http://pdbe.org/2req PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [http://www.ebi.ac.uk/pdbsum/2req PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	<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=2req ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 28:
	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 2req" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Propionibacterium shermanii van niel 1928]]
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	~~[[Category: Propionibacterium freudenreichii subsp. shermanii]]~~
	[[Category: Evans, P R]]		[[Category: Evans, P R]]
	[[Category: Mancia, F]]		[[Category: Mancia, F]]

OCA at 03:39, 25 December 2014

2014-12-25T03:39:23Z

← Older revision		Revision as of 03:39, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2REQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2REQ FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [http://www.ebi.ac.uk/pdbsum/2req 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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [http://www.ebi.ac.uk/pdbsum/2req PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/MUTB_PROFR MUTB_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates. [[http://www.uniprot.org/uniprot/MUTA_PROFR MUTA_PROFR]] Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Propionibacterium freudenreichii subsp. shermanii]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
	[[Category: Evans, P R.]]		[[Category: Evans, P R]]
	[[Category: Mancia, F.]]		[[Category: Mancia, F]]
	[[Category: Intramolecular transferase]]		[[Category: Intramolecular transferase]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Mutase]]		[[Category: Mutase]]

OCA at 08:18, 29 September 2014

2014-09-29T08:18:16Z

← Older revision		Revision as of 08:18, 29 September 2014
Line 1:		Line 1:
	[[Image:~~2req~~.~~png~~\|~~left~~\|~~200px~~]]		==METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE==
			<StructureSection load='2req' size='340' side='right' caption='[[2req]], [[Resolution\|resolution]] 2.50Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2REQ FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene><br>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MUTA, MUTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1752 Propionibacterium freudenreichii subsp. shermanii])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_mutase Methylmalonyl-CoA mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.2 5.4.99.2] </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=2req FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2req OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2req RCSB], [http://www.ebi.ac.uk/pdbsum/2req 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/re/2req_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: Methylmalonyl CoA mutase catalyses the interconversion of succinyl CoA and methylmalonyl CoA via a free radical mechanism. The enzyme belongs to a family of enzymes that catalyse intramolecular rearrangement reactions in which a group and a hydrogen atom on adjacent carbons are exchanged. These enzymes use the cofactor adenosylcobalamin (coenzyme B12) which breaks to form an adenosyl radical, thus initiating the reaction. Determination of the structure of substrate-free methylmalonyl CoA mutase was initiated to provide further insight into the mechanism of radical formation. RESULTS: We report here two structures of methylmalonyl CoA mutase from Propionibacterium shermanii. The first structure is of the enzyme in a nonproductive complex with CoA at 2.5 A resolution. This structure serves as a model for the substrate-free conformation of the enzyme, as it is very similar to the second much poorer 2.7 A resolution structure derived from a truly substrate-free crystal. The true substrate-free structure also shows the adenosyl group bound to the cobalt atom. Comparison of this structure with that of the previously reported complex of the enzyme with a substrate analogue shows that major conformational changes occur upon substrate binding. The substrate-binding site of the enzyme is located within a (beta alpha)8 TIM-barrel domain. In the absence of substrate, this TIM-barrel domain is split apart and the active site is accessible to solvent. When substrate binds, the barrel closes up with the substrate along its axis and the active site becomes completely buried. CONCLUSIONS: The closure of the active-site cavity upon substrate binding displaces the adenosyl group of the cofactor from the central cobalt atom into the active-site cavity. This triggers the formation of the free radical that initiates the rearrangement reaction. The TIM-barrel domain is substantially different from all others yet reported: in its unliganded form it is broken open, exposing the small hydrophilic sidechains which fill the centre. The typical barrel structure is only formed when substrate is bound.

	~~{{STRUCTURE_2req\| PDB=2req \| SCENE= }}~~		Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism.,Mancia F, Evans PR Structure. 1998 Jun 15;6(6):711-20. PMID:9655823<ref>PMID:9655823</ref>

	~~===METHYLMALONYL-COA MUTASE~~, ~~NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_9655823}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2req]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Propionibacterium_freudenreichii_subsp~~.~~_shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:009655823<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Propionibacterium freudenreichii subsp. shermanii]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]

OCA: Protected "2req" [edit=sysop:move=sysop]

2012-10-24T06:49:11Z

Protected "2req" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:49, 24 October 2012
(No difference)

OCA at 06:49, 24 October 2012

2012-10-24T06:49:09Z

← Older revision		Revision as of 06:49, 24 October 2012
Line 1:		Line 1:
	~~{{Seed}}~~
	[[Image:2req.png\|left\|200px]]		[[Image:2req.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2req", 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_2req\| PDB=2req \| SCENE= }}		{{STRUCTURE_2req\| PDB=2req \| SCENE= }}

	===METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE===		===METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_9655823}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 9655823 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_9655823}}		{{ABSTRACT_PUBMED_9655823}}

	==About this Structure==		==About this Structure==
	~~2REQ~~ is a 4 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA].		[[2req]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~9655823~~</ref><references group="xtra"/>		<ref group="xtra">PMID:009655823</ref><references group="xtra"/>
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Propionibacterium freudenreichii subsp. shermanii]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
Line 31:		Line 19:
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Mutase]]		[[Category: Mutase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:33:41 2009''~~

OCA at 03:33, 17 February 2009

2009-02-17T03:33:43Z

← Older revision		Revision as of 03:33, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	2REQ is a ~~[[Protein complex]]~~ structure of sequences from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA].		2REQ is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REQ OCA].

	==Reference==		==Reference==
	~~Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism., Mancia F, Evans PR, Structure. 1998 Jun 15;6(6):711-20.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/9655823 9655823]~~		<ref group="xtra">PMID:9655823</ref><references group="xtra"/>
	[[Category: Methylmalonyl-CoA mutase]]		[[Category: Methylmalonyl-CoA mutase]]
	[[Category: Propionibacterium freudenreichii subsp. shermanii]]		[[Category: Propionibacterium freudenreichii subsp. shermanii]]
	~~[[Category: Protein complex]]~~
	[[Category: Evans, P R.]]		[[Category: Evans, P R.]]
	[[Category: Mancia, F.]]		[[Category: Mancia, F.]]
Line 33:		Line 32:
	[[Category: Mutase]]		[[Category: Mutase]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 08~~:56:~~14 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:33:41 2009''