1fuy - Revision history

OCA at 11:16, 27 March 2024

OCA — Wed, 27 Mar 2024 11:16:49 GMT

←Older revision		Revision as of 11:16, 27 March 2024
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	<StructureSection load='1fuy' size='340' side='right'caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1fuy' size='340' side='right'caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fuy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fuy]] 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=1FUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUY FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FIP:5~~-~~FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>~~, ~~<scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.25Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1qop\|1qop]], [[1a50\|1a50]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [https://pdbe.org/1fuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [https://www.ebi.ac.uk/pdbsum/1fuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuy 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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [https://pdbe.org/1fuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [https://www.ebi.ac.uk/pdbsum/1fuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuy 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.
	== 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=1fuy 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=1fuy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	We determined the 2.25 A resolution crystal structure of the betaA169L/betaC170W mutant form of the tryptophan synthase alpha(2)beta(2) complex from Salmonella typhimurium complexed with the alpha-active site substrate analogue 5-fluoro-indole-propanol-phosphate to identify the structural basis for the changed kinetic properties of the mutant (Anderson, K. S., Kim, A. Y., Quillen, J. M., Sayers, E., Yang, X. J., and Miles, E. W. (1995) J. Biol. Chem. 270, 29936-29944). Comparison with the wild-type enzyme showed that the betaTrp(170) side chain occludes the tunnel connecting the alpha- and beta-active sites, explaining the accumulation of the intermediate indole during a single enzyme turnover. To prevent a steric clash between betaLeu(169) and betaGly(135), located in the beta-sheet of the COMM (communication) domain (betaGly(102)-betaGly(189)), the latter reorganizes. The changed COMM domain conformation results in a loss of the hydrogen bonding networks between the alpha- and beta-active sites, explaining the poor activation of the alpha-reaction upon formation of the aminoacrylate complex at the beta-active site. The 100-fold reduced affinity for serine seems to result from a movement of betaAsp(305) away from the beta-active site so that it cannot interact with the hydroxyl group of a pyridoxal phosphate-bound serine. The proposed structural dissection of the effects of each single mutation in the betaA169L/betaC170W mutant would explain the very different kinetics of this mutant and betaC170F.
-
-	Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase.,Weyand M, Schlichting I J Biol Chem. 2000 Dec 29;275(52):41058-63. PMID:11034989<ref>PMID:11034989</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1fuy" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Tryptophan synthase 3D structures\|Tryptophan synthase 3D structures]]		*[[Tryptophan synthase 3D structures\|Tryptophan synthase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Tryptophan synthase~~]]	+	[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-	[[Category: Schlichting, I]]	+	[[Category: Schlichting I]]
-	[[Category: Weyand, M]]	+	[[Category: Weyand M]]
-	~~[[Category: Carbon-oxygen lyase]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Pyridoxal phosphate]]~~	+
-	~~[[Category: Tryptophan biosynthesis~~]]	+

OCA at 09:01, 21 July 2021

OCA — Wed, 21 Jul 2021 09:01:03 GMT

←Older revision		Revision as of 09:01, 21 July 2021
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	<StructureSection load='1fuy' size='340' side='right'caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1fuy' size='340' side='right'caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fuy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1FUY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fuy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qop\|1qop]], [[1a50\|1a50]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qop\|1qop]], [[1a50\|1a50]]</div></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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [~~http~~://pdbe.org/1fuy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1fuy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuy 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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [https://pdbe.org/1fuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [https://www.ebi.ac.uk/pdbsum/1fuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuy 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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
-	*[[Tryptophan synthase\|Tryptophan synthase]]	+	*[[Tryptophan synthase 3D structures\|Tryptophan synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:50, 23 October 2019

OCA — Wed, 23 Oct 2019 08:50:16 GMT

←Older revision		Revision as of 08:50, 23 October 2019
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	==CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE==		==CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE==
-	<StructureSection load='1fuy' size='340' side='right' caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>	+	<StructureSection load='1fuy' size='340' side='right'caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fuy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FUY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fuy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FUY FirstGlance]. <br>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1fuy" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1fuy" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tryptophan synthase\|Tryptophan synthase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
	[[Category: Schlichting, I]]		[[Category: Schlichting, I]]

OCA at 06:33, 3 January 2018

OCA — Wed, 03 Jan 2018 06:33:25 GMT

←Older revision		Revision as of 06:33, 3 January 2018
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		+
	==CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE==		==CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE==
	<StructureSection load='1fuy' size='340' side='right' caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1fuy' size='340' side='right' caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qop\|1qop]], [[1a50\|1a50]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qop\|1qop]], [[1a50\|1a50]]</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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://pdbe.org/1fuy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy 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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://pdbe.org/1fuy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fu/1fuy_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fu/1fuy_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>
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1fuy" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1fuy" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Tryptophan synthase\|Tryptophan synthase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:24, 10 February 2016

OCA — Wed, 10 Feb 2016 06:24:58 GMT

←Older revision		Revision as of 06:24, 10 February 2016
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fuy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:14, 11 September 2015

OCA — Fri, 11 Sep 2015 06:14:53 GMT

←Older revision		Revision as of 06:14, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1fuy' size='340' side='right' caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='1fuy' size='340' side='right' caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fuy]] 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=1FUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FUY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fuy]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FUY FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qop\|1qop]], [[1a50\|1a50]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qop\|1qop]], [[1a50\|1a50]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRPA/TRPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy 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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://pdbe.org/1fuy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1fuy" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
	[[Category: Schlichting, I]]		[[Category: Schlichting, I]]

OCA at 12:25, 25 December 2014

OCA — Thu, 25 Dec 2014 12:25:45 GMT

←Older revision		Revision as of 12:25, 25 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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy 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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy 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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 20:27, 22 December 2014

OCA — Mon, 22 Dec 2014 20:27:48 GMT

OCA at 10:18, 28 September 2014

OCA — Sun, 28 Sep 2014 10:18:52 GMT

←Older revision		Revision as of 10:18, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1fuy.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE==
		+	<StructureSection load='1fuy' size='340' side='right' caption='[[1fuy]], [[Resolution\|resolution]] 2.25Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1fuy]] 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=1FUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FUY FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qop\|1qop]], [[1a50\|1a50]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRPA/TRPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy 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/fu/1fuy_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 determined the 2.25 A resolution crystal structure of the betaA169L/betaC170W mutant form of the tryptophan synthase alpha(2)beta(2) complex from Salmonella typhimurium complexed with the alpha-active site substrate analogue 5-fluoro-indole-propanol-phosphate to identify the structural basis for the changed kinetic properties of the mutant (Anderson, K. S., Kim, A. Y., Quillen, J. M., Sayers, E., Yang, X. J., and Miles, E. W. (1995) J. Biol. Chem. 270, 29936-29944). Comparison with the wild-type enzyme showed that the betaTrp(170) side chain occludes the tunnel connecting the alpha- and beta-active sites, explaining the accumulation of the intermediate indole during a single enzyme turnover. To prevent a steric clash between betaLeu(169) and betaGly(135), located in the beta-sheet of the COMM (communication) domain (betaGly(102)-betaGly(189)), the latter reorganizes. The changed COMM domain conformation results in a loss of the hydrogen bonding networks between the alpha- and beta-active sites, explaining the poor activation of the alpha-reaction upon formation of the aminoacrylate complex at the beta-active site. The 100-fold reduced affinity for serine seems to result from a movement of betaAsp(305) away from the beta-active site so that it cannot interact with the hydroxyl group of a pyridoxal phosphate-bound serine. The proposed structural dissection of the effects of each single mutation in the betaA169L/betaC170W mutant would explain the very different kinetics of this mutant and betaC170F.

-	~~{{STRUCTURE_1fuy\| PDB=1fuy \| SCENE= }}~~	+	Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase.,Weyand M, Schlichting I J Biol Chem. 2000 Dec 29;275(52):41058-63. PMID:11034989<ref>PMID:11034989</ref>

-	~~===CRYSTAL STRUCTURE OF BETAA169L~~/~~BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_11034989}}~~	+	==See Also==
-		+	*[[Tryptophan synthase\|Tryptophan synthase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1fuy~~]] 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=1FUY OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:011034989<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]

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

OCA — Wed, 21 Nov 2012 10:18:40 GMT

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

←Older revision

Revision as of 10:18, 21 November 2012

←Older revision		Revision as of 20:27, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fuy]] 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=1FUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FUY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fuy]] 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=1FUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FUY FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qop\|1qop]], [[1a50\|1a50]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qop\|1qop]], [[1a50\|1a50]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRPA/TRPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TRPA/TRPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy 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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
-	[[Category: Schlichting, I.]]	+	[[Category: Schlichting, I]]
-	[[Category: Weyand, M.]]	+	[[Category: Weyand, M]]
	[[Category: Carbon-oxygen lyase]]		[[Category: Carbon-oxygen lyase]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Pyridoxal phosphate]]		[[Category: Pyridoxal phosphate]]
	[[Category: Tryptophan biosynthesis]]		[[Category: Tryptophan biosynthesis]]