4kkx - Revision history

OCA at 06:07, 5 July 2023

OCA — Wed, 05 Jul 2023 06:07:33 GMT

←Older revision		Revision as of 06:07, 5 July 2023
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	<StructureSection load='4kkx' size='340' side='right'caption='[[4kkx]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='4kkx' size='340' side='right'caption='[[4kkx]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kkx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KKX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kkx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KKX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AQ3:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-3-[(2-HYDROXYPHENYL)AMINO]-D-ALANINE'>AQ3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F6F:2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL+DIHYDROGEN+PHOSPHATE'>F6F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.77Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4hpj\|4hpj]], [[2clm\|2clm]], [[2clf\|2clf]], [[2cle\|2cle]], [[3cep\|3cep]], [[3pr2\|3pr2]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AQ3:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-3-[(2-HYDROXYPHENYL)AMINO]-D-ALANINE'>AQ3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F6F:2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL+DIHYDROGEN+PHOSPHATE'>F6F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">trpA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892]), trpB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [https://pdbe.org/4kkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [https://www.ebi.ac.uk/pdbsum/4kkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkx 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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [https://pdbe.org/4kkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [https://www.ebi.ac.uk/pdbsum/4kkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate~~. [[https://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine~~.	+	[https://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus typhimurium loeffler 1892]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Tryptophan synthase~~]]	+	[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-	[[Category: Dunn~~, M F~~]]	+	[[Category: Dunn MF]]
-	[[Category: Fan, L]]	+	[[Category: Fan L]]
-	[[Category: Hilario, E]]	+	[[Category: Hilario E]]
-	[[Category: Mueller~~, L J~~]]	+	[[Category: Mueller LJ]]
-	[[Category: Niks, D]]	+	[[Category: Niks D]]
-	~~[[Category: 2-aminophenol quinonoid]]~~	+
-	~~[[Category: Allosteric enzyme]]~~	+
-	~~[[Category: Aromatic amino acid biosynthesis]]~~	+
-	~~[[Category: Biosynthesis]]~~	+
-	~~[[Category: Carbon-oxygen lyase]]~~	+
-	~~[[Category: F6f]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Lyase-lyase inhibitor complex]]~~	+
-	~~[[Category: Pyridoxal phosphate]]~~	+
-	~~[[Category: Tryptophan biosynthesis~~]]	+

OCA at 08:52, 29 September 2021

OCA — Wed, 29 Sep 2021 08:52:59 GMT

←Older revision		Revision as of 08:52, 29 September 2021
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	==Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site==		==Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site==
-	<StructureSection load='4kkx' size='340' side='right' caption='[[4kkx]], [[Resolution\|resolution]] 1.77Å' scene=''>	+	<StructureSection load='4kkx' size='340' side='right'caption='[[4kkx]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kkx]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4KKX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kkx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KKX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AQ3:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-3-[(2-HYDROXYPHENYL)AMINO]-D-ALANINE'>AQ3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F6F:2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL+DIHYDROGEN+PHOSPHATE'>F6F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AQ3:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-3-[(2-HYDROXYPHENYL)AMINO]-D-ALANINE'>AQ3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F6F:2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL+DIHYDROGEN+PHOSPHATE'>F6F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hpj\|4hpj]], [[2clm\|2clm]], [[2clf\|2clf]], [[2cle\|2cle]], [[3cep\|3cep]], [[3pr2\|3pr2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4hpj\|4hpj]], [[2clm\|2clm]], [[2clf\|2clf]], [[2cle\|2cle]], [[3cep\|3cep]], [[3pr2\|3pr2]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">trpA ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892]), trpB ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">trpA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892]), trpB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [~~http~~://pdbe.org/4kkx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4kkx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkx 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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [https://pdbe.org/4kkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [https://www.ebi.ac.uk/pdbsum/4kkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[~~http~~://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.	+	[[https://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[https://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Tryptophan synthase\|Tryptophan synthase]]	+	*[[Tryptophan synthase 3D structures\|Tryptophan synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Bacillus typhimurium loeffler 1892]]		[[Category: Bacillus typhimurium loeffler 1892]]
		+	[[Category: Large Structures]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
	[[Category: Dunn, M F]]		[[Category: Dunn, M F]]

OCA at 17:47, 4 August 2016

OCA — Thu, 04 Aug 2016 17:47:16 GMT

←Older revision		Revision as of 17:47, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site==		==Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site==
	<StructureSection load='4kkx' size='340' side='right' caption='[[4kkx]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='4kkx' size='340' side='right' caption='[[4kkx]], [[Resolution\|resolution]] 1.77Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">trpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892]), trpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">trpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892]), trpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [http://www.ebi.ac.uk/pdbsum/4kkx 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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [http://pdbe.org/4kkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [http://www.ebi.ac.uk/pdbsum/4kkx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4kkx" style="background-color:#fffaf0;"></div>

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

OCA at 17:48, 24 December 2014

OCA — Wed, 24 Dec 2014 17:48:14 GMT

←Older revision		Revision as of 17:48, 24 December 2014
Line 9:		Line 9:
	<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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [http://www.ebi.ac.uk/pdbsum/4kkx 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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [http://www.ebi.ac.uk/pdbsum/4kkx PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[http://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:29, 21 December 2014

OCA — Sun, 21 Dec 2014 17:29:46 GMT

←Older revision		Revision as of 17:29, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4kkx\| PDB=4kkx \| SCENE= }}~~	+	==Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site==
-	===Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site===	+	<StructureSection load='4kkx' size='340' side='right' caption='[[4kkx]], [[Resolution\|resolution]] 1.77Å' scene=''>
-	{{~~ABSTRACT_PUBMED_23952479}~~}	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4kkx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KKX FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AQ3:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-3-[(2-HYDROXYPHENYL)AMINO]-D-ALANINE'>AQ3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F6F:2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL+DIHYDROGEN+PHOSPHATE'>F6F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4hpj\|4hpj]], [[2clm\|2clm]], [[2clf\|2clf]], [[2cle\|2cle]], [[3cep\|3cep]], [[3pr2\|3pr2]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">trpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892]), trpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </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=4kkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kkx RCSB], [http://www.ebi.ac.uk/pdbsum/4kkx PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The allosteric regulation of substrate channeling in tryptophan synthase involves ligand-mediated allosteric signaling that switches the alpha- and beta-subunits between open (low activity) and closed (high activity) conformations. This switching prevents the escape of the common intermediate, indole, and synchronizes the alpha- and beta-catalytic cycles. (19)F NMR studies of bound alpha-site substrate analogues, N-(4'-trifluoromethoxybenzoyl)-2-aminoethyl phosphate (F6) and N-(4'-trifluoromethoxybenzenesulfonyl)-2-aminoethyl phosphate (F9), were found to be sensitive NMR probes of beta-subunit conformation. Both the internal and external aldimine F6 complexes gave a single bound peak at the same chemical shift, while alpha-aminoacrylate and quinonoid F6 complexes all gave a different bound peak shifted by +1.07 ppm. The F9 complexes exhibited similar behavior, but with a corresponding shift of -0.12 ppm. X-ray crystal structures show the F6 and F9 CF3 groups located at the alpha-beta subunit interface and report changes in both the ligand conformation and the surrounding protein microenvironment. Ab initio computational modeling suggests that the change in (19)F chemical shift results primarily from changes in the alpha-site ligand conformation. Structures of alpha-aminoacrylate F6 and F9 complexes and quinonoid F6 and F9 complexes show the alpha- and beta-subunits have closed conformations wherein access of ligands into the alpha- and beta-sites from solution is blocked. Internal and external aldimine structures show the alpha- and beta-subunits with closed and open global conformations, respectively. These results establish that beta-subunits exist in two global conformational states, designated open, where the beta-sites are freely accessible to substrates, and closed, where the beta-site portal into solution is blocked. Switching between these conformations is critically important for the alphabeta-catalytic cycle.

-	~~==Function==~~	+	Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states.,Niks D, Hilario E, Dierkers A, Ngo H, Borchardt D, Neubauer TJ, Fan L, Mueller LJ, Dunn MF Biochemistry. 2013 Sep 17;52(37):6396-411. doi: 10.1021/bi400795e. Epub 2013 Sep , 6. PMID:23952479<ref>PMID:23952479</ref>
-	~~[[http~~:~~//www~~.~~uniprot~~.~~org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3~~-~~phosphate~~. ~~[[http~~:/~~/www~~.~~uniprot~~.~~org~~/~~uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.~~	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4kkx]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4KKX OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023952479</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Tryptophan synthase\|Tryptophan synthase]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bacillus typhimurium loeffler 1892]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
-	[[Category: Dunn, M F.]]	+	[[Category: Dunn, M F]]
-	[[Category: Fan, L.]]	+	[[Category: Fan, L]]
-	[[Category: Hilario, E.]]	+	[[Category: Hilario, E]]
-	[[Category: Mueller, L J.]]	+	[[Category: Mueller, L J]]
-	[[Category: Niks, D.]]	+	[[Category: Niks, D]]
	[[Category: 2-aminophenol quinonoid]]		[[Category: 2-aminophenol quinonoid]]
	[[Category: Allosteric enzyme]]		[[Category: Allosteric enzyme]]

OCA at 12:09, 1 January 2014

OCA — Wed, 01 Jan 2014 12:09:12 GMT

←Older revision		Revision as of 12:09, 1 January 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4kkx\| PDB=4kkx \| SCENE= }}
		+	===Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site===
		+	{{ABSTRACT_PUBMED_23952479}}

-	The ~~entry 4kkx~~ is ~~ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[http://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.

-	~~Authors~~: ~~Hilario, E., Niks, D., Dunn, M.F~~.~~, Mueller, L~~.J.~~, Fan, L~~.	+	==About this Structure==
		+	[[4kkx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKX OCA].

-	~~Description~~: ~~Crystal structure of~~ Tryptophan ~~Synthase from Salmonella typhimurium with~~ 2-aminophenol quinonoid ~~in the beta site and the F6~~ inhibitor ~~in the alpha site~~	+	==Reference==
		+	<ref group="xtra">PMID:023952479</ref><references group="xtra"/><references/>
		+	[[Category: Tryptophan synthase]]
		+	[[Category: Dunn, M F.]]
		+	[[Category: Fan, L.]]
		+	[[Category: Hilario, E.]]
		+	[[Category: Mueller, L J.]]
		+	[[Category: Niks, D.]]
		+	[[Category: 2-aminophenol quinonoid]]
		+	[[Category: Allosteric enzyme]]
		+	[[Category: Aromatic amino acid biosynthesis]]
		+	[[Category: Biosynthesis]]
		+	[[Category: Carbon-oxygen lyase]]
		+	[[Category: F6f]]
		+	[[Category: Lyase]]
		+	[[Category: Lyase-lyase inhibitor complex]]
		+	[[Category: Pyridoxal phosphate]]
		+	[[Category: Tryptophan biosynthesis]]

OCA at 11:42, 19 June 2013

OCA — Wed, 19 Jun 2013 11:42:20 GMT

←Older revision		Revision as of 11:42, 19 June 2013
Line 5:		Line 5:
	Authors: Hilario, E., Niks, D., Dunn, M.F., Mueller, L.J., Fan, L.		Authors: Hilario, E., Niks, D., Dunn, M.F., Mueller, L.J., Fan, L.

-	Description: Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site.	+	Description: Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site

OCA: Protected "4kkx" [edit=sysop:move=sysop]

OCA — Thu, 16 May 2013 06:58:20 GMT

Protected "4kkx" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:58, 16 May 2013

OCA: New page: '''Unreleased structure''' The entry 4kkx is ON HOLD Authors: Hilario, E., Niks, D., Dunn, M.F., Mueller, L.J., Fan, L. Description: Crystal structure of Tryptophan Synthase from Salmo...

OCA — Thu, 16 May 2013 06:58:19 GMT

New page: '''Unreleased structure''' The entry 4kkx is ON HOLD Authors: Hilario, E., Niks, D., Dunn, M.F., Mueller, L.J., Fan, L. Description: Crystal structure of Tryptophan Synthase from Salmo...

New page

'''Unreleased structure'''

The entry 4kkx is ON HOLD

Authors: Hilario, E., Niks, D., Dunn, M.F., Mueller, L.J., Fan, L.

Description: Crystal structure of Tryptophan Synthase from Salmonella typhimurium with 2-aminophenol quinonoid in the beta site and the F6 inhibitor in the alpha site.