1i1q - Revision history

OCA at 07:32, 7 February 2024

OCA — Wed, 07 Feb 2024 07:32:03 GMT

←Older revision		Revision as of 07:32, 7 February 2024
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	<StructureSection load='1i1q' size='340' side='right'caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1i1q' size='340' side='right'caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1i1q]] 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=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</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]] 1.9Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [https://pdbe.org/1i1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [https://www.ebi.ac.uk/pdbsum/1i1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1q 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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [https://pdbe.org/1i1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [https://www.ebi.ac.uk/pdbsum/1i1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TRPE_SALTY TRPE_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.<ref>PMID:4358945</ref> [[https://www.uniprot.org/uniprot/TRPGD_SALTY TRPGD_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.<ref>PMID:4914739</ref>	+	[https://www.uniprot.org/uniprot/TRPE_SALTY TRPE_SALTY] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.<ref>PMID:4358945</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=1i1q 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=1i1q ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	We have determined the X-ray crystal structure of the cooperative anthranilate synthase heterotetramer from Salmonella typhimurium at 1.9 A resolution with the allosteric inhibitor l-tryptophan bound to a regulatory site in the TrpE subunit. Tryptophan binding orders a loop that in turn stabilizes the inactive T state of the enzyme by restricting closure of the active site cleft. Comparison with the structure of the unliganded, noncooperative anthranilate synthase heterotetramer from Sulfolobus solfataricus shows that the two homologs have completely different quarternary structures, even though their functional dimer pairs are structurally similar, consistent with differences in the cooperative behavior of the enzymes. The structural model rationalizes mutational and biochemical studies of the enzyme and establishes the structural differences between cooperative and noncooperative anthranilate synthase homologs.
-
-	Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.,Morollo AA, Eck MJ Nat Struct Biol. 2001 Mar;8(3):243-7. PMID:11224570<ref>PMID:11224570</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1i1q" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Anthranilate synthase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Eck, M J~~]]	+	[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-	[[Category: ~~Morollo, A A~~]]	+	[[Category: Eck MJ]]
-	[[Category: ~~Lyase]]~~	+	[[Category: Morollo AA]]
-	~~[[Category: Tryptophan biosynthesis~~]]	+

OCA at 10:55, 4 August 2021

OCA — Wed, 04 Aug 2021 10:55:57 GMT

←Older revision		Revision as of 10:55, 4 August 2021
Line 3:		Line 3:
	<StructureSection load='1i1q' size='340' side='right'caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1i1q' size='340' side='right'caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [~~http~~://pdbe.org/1i1q PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1i1q PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1q 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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [https://pdbe.org/1i1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [https://www.ebi.ac.uk/pdbsum/1i1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TRPE_SALTY TRPE_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.<ref>PMID:4358945</ref> [[~~http~~://www.uniprot.org/uniprot/TRPGD_SALTY TRPGD_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.<ref>PMID:4914739</ref>	+	[[https://www.uniprot.org/uniprot/TRPE_SALTY TRPE_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.<ref>PMID:4358945</ref> [[https://www.uniprot.org/uniprot/TRPGD_SALTY TRPGD_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.<ref>PMID:4914739</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:22, 30 October 2019

OCA — Wed, 30 Oct 2019 10:22:02 GMT

←Older revision		Revision as of 10:22, 30 October 2019
Line 1:		Line 1:

	==STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM==		==STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM==
-	<StructureSection load='1i1q' size='340' side='right' caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1i1q' size='340' side='right'caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>		<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>
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	</StructureSection>		</StructureSection>
	[[Category: Anthranilate synthase]]		[[Category: Anthranilate synthase]]
		+	[[Category: Large Structures]]
	[[Category: Eck, M J]]		[[Category: Eck, M J]]
	[[Category: Morollo, A A]]		[[Category: Morollo, A A]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Tryptophan biosynthesis]]		[[Category: Tryptophan biosynthesis]]

OCA at 09:23, 10 January 2018

OCA — Wed, 10 Jan 2018 09:23:17 GMT

←Older revision		Revision as of 09:23, 10 January 2018
Line 1:		Line 1:
		+
	==STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM==		==STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM==
	<StructureSection load='1i1q' size='340' side='right' caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1i1q' size='340' side='right' caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [http://pdbe.org/1i1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [http://www.ebi.ac.uk/pdbsum/1i1q 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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [http://pdbe.org/1i1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [http://www.ebi.ac.uk/pdbsum/1i1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/1i1q_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/1i1q_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 05:08, 10 February 2016

OCA — Wed, 10 Feb 2016 05:08:59 GMT

←Older revision		Revision as of 05:08, 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=1i1q ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 05:41, 11 September 2015

OCA — Fri, 11 Sep 2015 05:41:01 GMT

←Older revision		Revision as of 05:41, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1i1q' size='340' side='right' caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1i1q' size='340' side='right' caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure ~~with sequence from [http://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=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [http://www.ebi.ac.uk/pdbsum/1i1q 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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [http://pdbe.org/1i1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [http://www.ebi.ac.uk/pdbsum/1i1q PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/TRPE_SALTY TRPE_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.<ref>PMID:4358945</ref> [[http://www.uniprot.org/uniprot/~~TRPG_SALTY TRPG_SALTY~~]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.<ref>PMID:4914739</ref>	+	[[http://www.uniprot.org/uniprot/TRPE_SALTY TRPE_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.<ref>PMID:4358945</ref> [[http://www.uniprot.org/uniprot/TRPGD_SALTY TRPGD_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.<ref>PMID:4914739</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 1i1q" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Anthranilate synthase]]		[[Category: Anthranilate synthase]]
-	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
	[[Category: Eck, M J]]		[[Category: Eck, M J]]
	[[Category: Morollo, A A]]		[[Category: Morollo, A A]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Tryptophan biosynthesis]]		[[Category: Tryptophan biosynthesis]]

OCA at 12:00, 25 December 2014

OCA — Thu, 25 Dec 2014 12:00:13 GMT

←Older revision		Revision as of 12:00, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure with sequence from [http://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=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>		<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure with sequence from [http://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=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [http://www.ebi.ac.uk/pdbsum/1i1q 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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [http://www.ebi.ac.uk/pdbsum/1i1q PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TRPE_SALTY TRPE_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.<ref>PMID:4358945</ref> [[http://www.uniprot.org/uniprot/TRPG_SALTY TRPG_SALTY]] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.<ref>PMID:4914739</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	[[Category: Anthranilate synthase]]		[[Category: Anthranilate synthase]]
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
-	[[Category: Eck, M J.]]	+	[[Category: Eck, M J]]
-	[[Category: Morollo, A A.]]	+	[[Category: Morollo, A A]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Tryptophan biosynthesis]]		[[Category: Tryptophan biosynthesis]]

OCA at 09:35, 28 September 2014

OCA — Sun, 28 Sep 2014 09:35:53 GMT

←Older revision		Revision as of 09:35, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1i1q.~~png\|left~~\|200px]]	+	==STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM==
		+	<StructureSection load='1i1q' size='340' side='right' caption='[[1i1q]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1i1q]] is a 2 chain structure with sequence from [http://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=1I1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1Q FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] </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=1i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i1q RCSB], [http://www.ebi.ac.uk/pdbsum/1i1q 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/i1/1i1q_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 determined the X-ray crystal structure of the cooperative anthranilate synthase heterotetramer from Salmonella typhimurium at 1.9 A resolution with the allosteric inhibitor l-tryptophan bound to a regulatory site in the TrpE subunit. Tryptophan binding orders a loop that in turn stabilizes the inactive T state of the enzyme by restricting closure of the active site cleft. Comparison with the structure of the unliganded, noncooperative anthranilate synthase heterotetramer from Sulfolobus solfataricus shows that the two homologs have completely different quarternary structures, even though their functional dimer pairs are structurally similar, consistent with differences in the cooperative behavior of the enzymes. The structural model rationalizes mutational and biochemical studies of the enzyme and establishes the structural differences between cooperative and noncooperative anthranilate synthase homologs.

-	~~{{STRUCTURE_1i1q\| PDB=1i1q \| SCENE= }}~~	+	Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.,Morollo AA, Eck MJ Nat Struct Biol. 2001 Mar;8(3):243-7. PMID:11224570<ref>PMID:11224570</ref>

-	~~===STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11224570}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1i1q]] is~~ a ~~2 chain structure with sequence from [http://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=1I1Q OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:011224570<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Anthranilate synthase]]		[[Category: Anthranilate synthase]]
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]

OCA: Protected "1i1q" [edit=sysop:move=sysop]

OCA — Wed, 21 Nov 2012 16:07:10 GMT

Protected "1i1q" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:07, 21 November 2012

OCA at 16:07, 21 November 2012

OCA — Wed, 21 Nov 2012 16:07:07 GMT

←Older revision		Revision as of 16:07, 21 November 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1i1q.png\|left\|200px]]		[[Image:1i1q.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1i1q", 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.
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	{{STRUCTURE_1i1q\| PDB=1i1q \| SCENE= }}		{{STRUCTURE_1i1q\| PDB=1i1q \| SCENE= }}

	===STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM===		===STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_11224570}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 11224570 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_11224570}}		{{ABSTRACT_PUBMED_11224570}}

	==About this Structure==		==About this Structure==
-	~~1I1Q~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/~~Salmonella_typhimurium~~ Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA].	+	[[1i1q]] is a 2 chain structure with sequence from [http://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=1I1Q OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11224570~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011224570</ref><references group="xtra"/>
	[[Category: Anthranilate synthase]]		[[Category: Anthranilate synthase]]
-	[[Category: Salmonella typhimurium]]	+	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
	[[Category: Eck, M J.]]		[[Category: Eck, M J.]]
	[[Category: Morollo, A A.]]		[[Category: Morollo, A A.]]
		+	[[Category: Lyase]]
	[[Category: Tryptophan biosynthesis]]		[[Category: Tryptophan biosynthesis]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:40:42 2009''