2cht - Revision history

OCA at 09:18, 14 February 2024

2024-02-14T09:18:03Z

← Older revision		Revision as of 09:18, 14 February 2024
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	<StructureSection load='2cht' size='340' side='right'caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2cht' size='340' side='right'caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"vibrio_subtilis"_ehrenberg_1835 "vibrio~~ subtilis~~" ehrenberg 1835~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHT FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=TSA:8-HYDROXY~~-2~~-OXA-BICYCLO[3~~.~~3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</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]] 2.2Å</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks'>~~[~~https://en~~.~~wikipedia~~.~~org/wiki/Chorismate_mutase Chorismate mutase~~], ~~with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5]~~ </~~span~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [https://pdbe.org/2cht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [https://www.ebi.ac.uk/pdbsum/2cht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cht 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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [https://pdbe.org/2cht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [https://www.ebi.ac.uk/pdbsum/2cht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cht ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/AROH_BACSU AROH_BACSU]] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>		[https://www.uniprot.org/uniprot/AROH_BACSU AROH_BACSU] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>
	== 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=2cht 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=2cht ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-A crystal structure of the monofunctional enzyme from Bacillus subtilis. The structure determination process was an unusual one, involving 12 monomers of the enzyme in the asymmetric unit. This structure was solved by the multiple isomorphous replacement method with partial structure phase combination and molecular averaging. The final model, which includes 1380 residues and 522 water molecules in an asymmetric unit, has been refined at 1.9 A and the current crystallographic R value is 0.201. The B. subtilis chorismate mutase is a homotrimer, with beta-sheets from each monomer packing to form the core of a pseudo-alpha beta-barrel with helices on the outside of the trimer. In addition, the active sites have been located by using data from a complex with an endo-oxabicyclic inhibitor that mimics the transition state of the reaction. The structure of this complex has been refined to 2.2 A with a current R value of 0.182 for a model that includes 1388 residues, 12 inhibitor molecules, and 530 water molecules in the asymmetric unit. In each trimer, three equivalent active sites are located at the interfaces of two adjacent subunits.

	~~Crystal~~ structures of ~~the monofunctional~~ chorismate mutase ~~from Bacillus subtilis and its complex with a transition state analog.,Chook YM, Ke H, Lipscomb WN Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8600-3. PMID:8378335<ref>PMID:8378335</ref>~~		==See Also==
			*[[3D structures of chorismate mutase\|3D structures of chorismate mutase]]
	~~From MEDLINE®/PubMed®, a database~~ of ~~the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2cht" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Vibrio~~ subtilis ~~ehrenberg 1835]]~~		[[Category: Bacillus subtilis]]
	~~[[Category: Chorismate mutase~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Chook~~, Y M~~]]		[[Category: Chook YM]]
	[[Category: Ke, H]]		[[Category: Ke H]]
	[[Category: Lipscomb~~, W N]]~~		[[Category: Lipscomb WN]]
	~~[[Category: Isomerase~~]]

OCA at 16:37, 3 November 2021

2021-11-03T16:37:48Z

← Older revision		Revision as of 16:37, 3 November 2021
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	<StructureSection load='2cht' size='340' side='right'caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2cht' size='340' side='right'caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CHT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [~~http~~://pdbe.org/2cht PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2cht PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2cht 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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [https://pdbe.org/2cht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [https://www.ebi.ac.uk/pdbsum/2cht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cht ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/AROH_BACSU AROH_BACSU]] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>		[[https://www.uniprot.org/uniprot/AROH_BACSU AROH_BACSU]] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 19:29, 11 December 2019

2019-12-11T19:29:24Z

← Older revision		Revision as of 19:29, 11 December 2019
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	==CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG==		==CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG==
	<StructureSection load='2cht' size='340' side='right' caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2cht' size='340' side='right'caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/2cht_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/2cht_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>
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	[[Category: Vibrio subtilis ehrenberg 1835]]		[[Category: Vibrio subtilis ehrenberg 1835]]
	[[Category: Chorismate mutase]]		[[Category: Chorismate mutase]]
			[[Category: Large Structures]]
	[[Category: Chook, Y M]]		[[Category: Chook, Y M]]
	[[Category: Ke, H]]		[[Category: Ke, H]]
	[[Category: Lipscomb, W N]]		[[Category: Lipscomb, W N]]
	[[Category: Isomerase]]		[[Category: Isomerase]]

OCA at 07:05, 29 November 2017

2017-11-29T07:05:25Z

← Older revision		Revision as of 07:05, 29 November 2017
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	==CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG==		==CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG==
	<StructureSection load='2cht' size='340' side='right' caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2cht' size='340' side='right' caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"~~bacillus_globigii~~"~~_migula_1900~~ "~~bacillus globigii~~" ~~migula 1900~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [http://pdbe.org/2cht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [http://www.ebi.ac.uk/pdbsum/2cht 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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [http://pdbe.org/2cht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [http://www.ebi.ac.uk/pdbsum/2cht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cht ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		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=2cht ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus globigii migula 1900~~]]		[[Category: Vibrio subtilis ehrenberg 1835]]
	[[Category: Chorismate mutase]]		[[Category: Chorismate mutase]]
	[[Category: Chook, Y M]]		[[Category: Chook, Y M]]

OCA at 12:17, 11 September 2015

2015-09-11T12:17:36Z

← Older revision		Revision as of 12:17, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2cht' size='340' side='right' caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='2cht' size='340' side='right' caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_subtilis Bacillus subtilis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [http://www.ebi.ac.uk/pdbsum/2cht 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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [http://pdbe.org/2cht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [http://www.ebi.ac.uk/pdbsum/2cht PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/~~CHMU_BACSU CHMU_BACSU~~]] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>		[[http://www.uniprot.org/uniprot/AROH_BACSU AROH_BACSU]] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2cht" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Bacillus ~~subtilis~~]]		[[Category: Bacillus globigii migula 1900]]
	[[Category: Chorismate mutase]]		[[Category: Chorismate mutase]]
	[[Category: Chook, Y M]]		[[Category: Chook, Y M]]

OCA at 16:20, 25 December 2014

2014-12-25T16:20:31Z

← Older revision		Revision as of 16:20, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [http://www.ebi.ac.uk/pdbsum/2cht 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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [http://www.ebi.ac.uk/pdbsum/2cht PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/CHMU_BACSU CHMU_BACSU]] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Chorismate mutase]]		[[Category: Chorismate mutase]]
	[[Category: Chook, Y M.]]		[[Category: Chook, Y M]]
	[[Category: Ke, H.]]		[[Category: Ke, H]]
	[[Category: Lipscomb, W N.]]		[[Category: Lipscomb, W N]]
	[[Category: Isomerase]]		[[Category: Isomerase]]

OCA at 01:58, 30 September 2014

2014-09-30T01:58:00Z

← Older revision		Revision as of 01:58, 30 September 2014
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	[[Image:~~2cht~~.~~png~~\|~~left~~\|~~200px~~]]		==CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG==
			<StructureSection load='2cht' size='340' side='right' caption='[[2cht]], [[Resolution\|resolution]] 2.20Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CHT FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene><br>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </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=2cht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cht RCSB], [http://www.ebi.ac.uk/pdbsum/2cht 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/ch/2cht_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 ==
			We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-A crystal structure of the monofunctional enzyme from Bacillus subtilis. The structure determination process was an unusual one, involving 12 monomers of the enzyme in the asymmetric unit. This structure was solved by the multiple isomorphous replacement method with partial structure phase combination and molecular averaging. The final model, which includes 1380 residues and 522 water molecules in an asymmetric unit, has been refined at 1.9 A and the current crystallographic R value is 0.201. The B. subtilis chorismate mutase is a homotrimer, with beta-sheets from each monomer packing to form the core of a pseudo-alpha beta-barrel with helices on the outside of the trimer. In addition, the active sites have been located by using data from a complex with an endo-oxabicyclic inhibitor that mimics the transition state of the reaction. The structure of this complex has been refined to 2.2 A with a current R value of 0.182 for a model that includes 1388 residues, 12 inhibitor molecules, and 530 water molecules in the asymmetric unit. In each trimer, three equivalent active sites are located at the interfaces of two adjacent subunits.

	~~{{STRUCTURE_2cht\| PDB=2cht \| SCENE= }}~~		Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog.,Chook YM, Ke H, Lipscomb WN Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8600-3. PMID:8378335<ref>PMID:8378335</ref>

	~~===CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_8378335}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2cht]] is~~ a ~~12 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bacillus_subtilis Bacillus subtilis]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:008378335<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Chorismate mutase]]		[[Category: Chorismate mutase]]

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

2013-01-06T11:11:39Z

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

← Older revision	Revision as of 11:11, 6 January 2013
(No difference)

OCA at 11:11, 6 January 2013

2013-01-06T11:11:34Z

← Older revision		Revision as of 11:11, 6 January 2013
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	~~{{Seed}}~~
	[[Image:2cht.png\|left\|200px]]		[[Image:2cht.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2cht", 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_2cht\| PDB=2cht \| SCENE= }}		{{STRUCTURE_2cht\| PDB=2cht \| SCENE= }}

	===CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG===		===CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_8378335}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 8378335 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_8378335}}		{{ABSTRACT_PUBMED_8378335}}

	==About this Structure==		==About this Structure==
	~~2CHT~~ is a 12 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA].		[[2cht]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~8378335~~</ref><references group="xtra"/>		<ref group="xtra">PMID:008378335</ref><references group="xtra"/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Chorismate mutase]]		[[Category: Chorismate mutase]]
Line 30:		Line 18:
	[[Category: Lipscomb, W N.]]		[[Category: Lipscomb, W N.]]
	[[Category: Isomerase]]		[[Category: Isomerase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:35:49 2009''~~

OCA at 19:35, 17 February 2009

2009-02-17T19:35:50Z

← Older revision		Revision as of 19:35, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	2CHT is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA].		2CHT is a 12 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA].

	==Reference==		==Reference==
	Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog., Chook YM, Ke H, Lipscomb WN, Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8600-3. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/8378335 8378335]~~		<ref group="xtra">PMID:8378335</ref><references group="xtra"/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Chorismate mutase]]		[[Category: Chorismate mutase]]
	~~[[Category: Single protein]]~~
	[[Category: Chook, Y M.]]		[[Category: Chook, Y M.]]
	[[Category: Ke, H.]]		[[Category: Ke, H.]]
Line 32:		Line 31:
	[[Category: Isomerase]]		[[Category: Isomerase]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue ~~Jul 29 05~~:43:~~58 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:35:49 2009''