1m1b - Revision history

OCA at 07:38, 14 February 2024

OCA — Wed, 14 Feb 2024 07:38:29 GMT

←Older revision		Revision as of 07:38, 14 February 2024
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	<StructureSection load='1m1b' size='340' side='right'caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1m1b' size='340' side='right'caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Blue_mussel Blue mussel~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1B FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1B FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~, ~~<scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</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]] 2.25Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https:~~/~~/en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase]~~, ~~with EC number [https~~:~~//www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [https://pdbe.org/1m1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [https://www.ebi.ac.uk/pdbsum/1m1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1b 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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [https://pdbe.org/1m1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [https://www.ebi.ac.uk/pdbsum/1m1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1b ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PEPM_MYTED PEPM_MYTED]] Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).	+	[https://www.uniprot.org/uniprot/PEPM_MYTED PEPM_MYTED] Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1m1b 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=1m1b ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The crystal structure of PEP mutase from Mytilus edulis in complex with a substrate-analogue inhibitor, sulfopyruvate S-pyr (K(i) = 22 microM), has been determined at 2.25 A resolution. Mg(II)-S-pyr binds in the alpha/beta barrel's central channel, at the C-termini of the beta-strands. The binding mode of S-pyr's pyruvyl moiety resembles the binding mode of oxalate seen earlier. The location of the sulfo group of S-pyr is postulated to mimic the phosphonyl group of the product phosphonopyruvate (P-pyr). This sulfo group interacts with the guanidinium group of Arg159, but it is not aligned for nucleopilic attack by neighboring basic amino side chains. Kinetic analysis of site directed mutants, probing the key active site residues Asp58, Arg159, Asn122, and His190 correlate well with the structural information. The results presented here rule out a phosphoryl transfer mechanism involving a double displacement, and suggest instead that PEP mutase catalysis proceeds via a dissociative mechanism in which the pyruvyl C(3) adds to the same face of the phosphorus from which the C(2)O departs. We propose that Arg159 and His190 serve to hold the phosphoryl/metaphosphate/phosphonyl group stationary along the reaction pathway, while the pyruvyl C(1)-C(2) bond rotates upon formation of the metaphosphate. In agreement with published data, the phosphoryl group transfer occurs on the Si-face of PEP with retention of configuration at phosphorus.
-
-	Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants.,Liu S, Lu Z, Jia Y, Dunaway-Mariano D, Herzberg O Biochemistry. 2002 Aug 13;41(32):10270-6. PMID:12162742<ref>PMID:12162742</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1m1b" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Blue mussel]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Phosphoenolpyruvate mutase~~]]	+	[[Category: Mytilus edulis]]
-	[[Category: Dunaway-Mariano, D]]	+	[[Category: Dunaway-Mariano D]]
-	[[Category: Herzberg, O]]	+	[[Category: Herzberg O]]
-	[[Category: Jia, Y]]	+	[[Category: Jia Y]]
-	[[Category: Liu, S]]	+	[[Category: Liu S]]
-	[[Category: Lu, Z]]	+	[[Category: Lu Z]]
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Pep mutase]]~~	+
-	~~[[Category: Sulfopyruvate~~]]	+

OCA at 06:52, 18 August 2021

OCA — Wed, 18 Aug 2021 06:52:11 GMT

←Older revision		Revision as of 06:52, 18 August 2021
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	<StructureSection load='1m1b' size='340' side='right'caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1m1b' size='340' side='right'caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Blue_mussel Blue mussel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1M1B FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Blue_mussel Blue mussel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1B FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [~~http~~://pdbe.org/1m1b PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1m1b PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1b 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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [https://pdbe.org/1m1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [https://www.ebi.ac.uk/pdbsum/1m1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1b ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PEPM_MYTED PEPM_MYTED]] Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).	+	[[https://www.uniprot.org/uniprot/PEPM_MYTED PEPM_MYTED]] Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 12:04, 13 November 2019

OCA — Wed, 13 Nov 2019 12:04:06 GMT

←Older revision		Revision as of 12:04, 13 November 2019
Line 1:		Line 1:

	==Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate==		==Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate==
-	<StructureSection load='1m1b' size='340' side='right' caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>	+	<StructureSection load='1m1b' size='340' side='right'caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Blue_mussel Blue mussel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1B FirstGlance]. <br>		<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Blue_mussel Blue mussel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1B FirstGlance]. <br>
Line 34:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Blue mussel]]		[[Category: Blue mussel]]
		+	[[Category: Large Structures]]
	[[Category: Phosphoenolpyruvate mutase]]		[[Category: Phosphoenolpyruvate mutase]]
	[[Category: Dunaway-Mariano, D]]		[[Category: Dunaway-Mariano, D]]

OCA at 07:41, 31 January 2018

OCA — Wed, 31 Jan 2018 07:41:43 GMT

←Older revision		Revision as of 07:41, 31 January 2018
Line 1:		Line 1:
		+
	==Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate==		==Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate==
	<StructureSection load='1m1b' size='340' side='right' caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1m1b' size='340' side='right' caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [http://pdbe.org/1m1b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [http://www.ebi.ac.uk/pdbsum/1m1b 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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [http://pdbe.org/1m1b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [http://www.ebi.ac.uk/pdbsum/1m1b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1b 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/m1/1m1b_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m1b_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 07:24, 10 February 2016

OCA — Wed, 10 Feb 2016 07:24:45 GMT

←Older revision		Revision as of 07:24, 10 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=1m1b ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:40, 11 September 2015

OCA — Fri, 11 Sep 2015 06:40:24 GMT

←Older revision		Revision as of 06:40, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1m1b' size='340' side='right' caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1m1b' size='340' side='right' caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mytilus_edulis Mytilus edulis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1B FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Blue_mussel Blue mussel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1B FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [http://www.ebi.ac.uk/pdbsum/1m1b 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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [http://pdbe.org/1m1b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [http://www.ebi.ac.uk/pdbsum/1m1b 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 1m1b" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mytilus edulis~~]]	+	[[Category: Blue mussel]]
	[[Category: Phosphoenolpyruvate mutase]]		[[Category: Phosphoenolpyruvate mutase]]
	[[Category: Dunaway-Mariano, D]]		[[Category: Dunaway-Mariano, D]]

OCA at 12:42, 25 December 2014

OCA — Thu, 25 Dec 2014 12:42:48 GMT

←Older revision		Revision as of 12:42, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1B FirstGlance]. <br>		<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1B FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [http://www.ebi.ac.uk/pdbsum/1m1b 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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [http://www.ebi.ac.uk/pdbsum/1m1b PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PEPM_MYTED PEPM_MYTED]] Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	[[Category: Mytilus edulis]]		[[Category: Mytilus edulis]]
	[[Category: Phosphoenolpyruvate mutase]]		[[Category: Phosphoenolpyruvate mutase]]
-	[[Category: Dunaway-Mariano, D.]]	+	[[Category: Dunaway-Mariano, D]]
-	[[Category: Herzberg, O.]]	+	[[Category: Herzberg, O]]
-	[[Category: Jia, Y.]]	+	[[Category: Jia, Y]]
-	[[Category: Liu, S.]]	+	[[Category: Liu, S]]
-	[[Category: Lu, Z.]]	+	[[Category: Lu, Z]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Pep mutase]]		[[Category: Pep mutase]]
-	[[Category: Phosphoenolpyruvate mutase]]
	[[Category: Sulfopyruvate]]		[[Category: Sulfopyruvate]]

OCA at 14:49, 28 September 2014

OCA — Sun, 28 Sep 2014 14:49:11 GMT

←Older revision		Revision as of 14:49, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1m1b.~~png\|left~~\|200px]]	+	==Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate==
		+	<StructureSection load='1m1b' size='340' side='right' caption='[[1m1b]], [[Resolution\|resolution]] 2.25Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1B FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] </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=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [http://www.ebi.ac.uk/pdbsum/1m1b 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/m1/1m1b_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 ==
		+	The crystal structure of PEP mutase from Mytilus edulis in complex with a substrate-analogue inhibitor, sulfopyruvate S-pyr (K(i) = 22 microM), has been determined at 2.25 A resolution. Mg(II)-S-pyr binds in the alpha/beta barrel's central channel, at the C-termini of the beta-strands. The binding mode of S-pyr's pyruvyl moiety resembles the binding mode of oxalate seen earlier. The location of the sulfo group of S-pyr is postulated to mimic the phosphonyl group of the product phosphonopyruvate (P-pyr). This sulfo group interacts with the guanidinium group of Arg159, but it is not aligned for nucleopilic attack by neighboring basic amino side chains. Kinetic analysis of site directed mutants, probing the key active site residues Asp58, Arg159, Asn122, and His190 correlate well with the structural information. The results presented here rule out a phosphoryl transfer mechanism involving a double displacement, and suggest instead that PEP mutase catalysis proceeds via a dissociative mechanism in which the pyruvyl C(3) adds to the same face of the phosphorus from which the C(2)O departs. We propose that Arg159 and His190 serve to hold the phosphoryl/metaphosphate/phosphonyl group stationary along the reaction pathway, while the pyruvyl C(1)-C(2) bond rotates upon formation of the metaphosphate. In agreement with published data, the phosphoryl group transfer occurs on the Si-face of PEP with retention of configuration at phosphorus.

-	~~{{STRUCTURE_1m1b\| PDB=1m1b \| SCENE= }}~~	+	Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants.,Liu S, Lu Z, Jia Y, Dunaway-Mariano D, Herzberg O Biochemistry. 2002 Aug 13;41(32):10270-6. PMID:12162742<ref>PMID:12162742</ref>

-	~~===Crystal Structure~~ of ~~Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12162742}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1m1b]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Mytilus_edulis Mytilus edulis]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:012162742<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Mytilus edulis]]		[[Category: Mytilus edulis]]
	[[Category: Phosphoenolpyruvate mutase]]		[[Category: Phosphoenolpyruvate mutase]]

OCA: Protected "1m1b" [edit=sysop:move=sysop]

OCA — Wed, 05 Dec 2012 20:35:55 GMT

Protected "1m1b" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:35, 5 December 2012

OCA at 20:35, 5 December 2012

OCA — Wed, 05 Dec 2012 20:35:51 GMT

←Older revision		Revision as of 20:35, 5 December 2012
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-	{{Seed}}
	[[Image:1m1b.png\|left\|200px]]		[[Image:1m1b.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1m1b", 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_1m1b\| PDB=1m1b \| SCENE= }}		{{STRUCTURE_1m1b\| PDB=1m1b \| SCENE= }}

	===Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate===		===Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12162742}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12162742 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_12162742}}		{{ABSTRACT_PUBMED_12162742}}

	==About this Structure==		==About this Structure==
-	~~1M1B~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA].	+	[[1m1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12162742~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012162742</ref><references group="xtra"/>
	[[Category: Mytilus edulis]]		[[Category: Mytilus edulis]]
	[[Category: Phosphoenolpyruvate mutase]]		[[Category: Phosphoenolpyruvate mutase]]
Line 31:		Line 19:
	[[Category: Liu, S.]]		[[Category: Liu, S.]]
	[[Category: Lu, Z.]]		[[Category: Lu, Z.]]
		+	[[Category: Isomerase]]
	[[Category: Pep mutase]]		[[Category: Pep mutase]]
	[[Category: Phosphoenolpyruvate mutase]]		[[Category: Phosphoenolpyruvate mutase]]
	[[Category: Sulfopyruvate]]		[[Category: Sulfopyruvate]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:29:04 2009''