1kfk - Revision history

OCA at 08:00, 3 April 2024

2024-04-03T08:00:17Z

←Older revision		Revision as of 08:00, 3 April 2024
Line 3:		Line 3:
	<StructureSection load='1kfk' size='340' side='right'caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1kfk' size='340' side='right'caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kfk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ ] and [https://en.wikipedia.org/wiki/~~Salty Salty~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kfk]] 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] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFK FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<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]] 2.4Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1bks\|1bks]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [https://pdbe.org/1kfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [https://www.ebi.ac.uk/pdbsum/1kfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfk 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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [https://pdbe.org/1kfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [https://www.ebi.ac.uk/pdbsum/1kfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfk 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=1kfk 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=1kfk ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The catalytic activity and substrate channeling of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is regulated by allosteric interactions that modulate the switching of the enzyme between open, low activity and closed, high activity states during the catalytic cycle. The highly conserved alphaThr183 residue is part of loop alphaL6 and is located next to the alpha-active site and forms part of the alpha-beta subunit interface. The role of the interactions of alphaThr183 in alpha-site catalysis and allosteric regulation was investigated by analyzing the kinetics and crystal structures of the isosteric mutant alphaThr183Val. The mutant displays strongly impaired allosteric alpha-beta communication, and the catalytic activity of the alpha-reaction is reduced one hundred fold, whereas the beta-activity is not affected. The structural work establishes that the basis for the missing inter-subunit signaling is the lack of loop alphaL6 closure even in the presence of the alpha-subunit ligands, 3-indolyl-D-glycerol 3'-phosphate, or 3-indolylpropanol 3'-phosphate. The structural basis for the reduced alpha-activity has its origins in the missing hydrogen bond between alphaThr183 and the catalytic residue, alphaAsp60.
-
-	On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase.,Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I J Mol Biol. 2002 Dec 6;324(4):677-90. PMID:12460570<ref>PMID:12460570</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1kfk" 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: ~~Salty~~]]	+	[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-	[[Category: ~~Tryptophan synthase~~]]	+	[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
-	[[Category: Arac, D]]	+	[[Category: Arac D]]
-	[[Category: Dunn~~, M F~~]]	+	[[Category: Dunn MF]]
-	[[Category: Kulik, V]]	+	[[Category: Kulik V]]
-	[[Category: Niks, D]]	+	[[Category: Niks D]]
-	[[Category: Schlichting, I]]	+	[[Category: Schlichting I]]
-	[[Category: Seidel, R]]	+	[[Category: Seidel R]]
-	[[Category: Weyand, M]]	+	[[Category: Weyand M]]
-	~~[[Category: Carbon-oxygen lyase]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Pyridoxal phosphate]]~~	+
-	~~[[Category: Tryptophan biosynthesis~~]]	+

OCA at 06:53, 11 August 2021

2021-08-11T06:53:19Z

←Older revision		Revision as of 06:53, 11 August 2021
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	<StructureSection load='1kfk' size='340' side='right'caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1kfk' size='340' side='right'caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kfk]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/ ] and [~~http~~://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1KFK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kfk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ ] and [https://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=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">[[1bks\|1bks]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bks\|1bks]]</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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [~~http~~://pdbe.org/1kfk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1kfk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfk 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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [https://pdbe.org/1kfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [https://www.ebi.ac.uk/pdbsum/1kfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfk 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]]
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Tryptophan synthase\|Tryptophan synthase]]	+	*[[Tryptophan synthase 3D structures\|Tryptophan synthase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:32, 6 November 2019

2019-11-06T09:32:32Z

←Older revision		Revision as of 09:32, 6 November 2019
Line 1:		Line 1:

	==Crystal structure of Tryptophan Synthase From Salmonella Typhimurium==		==Crystal structure of Tryptophan Synthase From Salmonella Typhimurium==
-	<StructureSection load='1kfk' size='340' side='right' caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='1kfk' size='340' side='right'caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1kfk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFK FirstGlance]. <br>		<table><tr><td colspan='2'>[[1kfk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFK FirstGlance]. <br>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1kfk" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1kfk" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tryptophan synthase\|Tryptophan synthase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Salty]]		[[Category: Salty]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]

OCA at 21:39, 24 January 2018

2018-01-24T21:39:03Z

←Older revision		Revision as of 21:39, 24 January 2018
Line 1:		Line 1:
		+
	==Crystal structure of Tryptophan Synthase From Salmonella Typhimurium==		==Crystal structure of Tryptophan Synthase From Salmonella Typhimurium==
	<StructureSection load='1kfk' size='340' side='right' caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1kfk' size='340' side='right' caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bks\|1bks]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bks\|1bks]]</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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [http://pdbe.org/1kfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [http://www.ebi.ac.uk/pdbsum/1kfk 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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [http://pdbe.org/1kfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [http://www.ebi.ac.uk/pdbsum/1kfk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfk 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/kf/1kfk_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/1kfk_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 1kfk" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1kfk" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Tryptophan synthase\|Tryptophan synthase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:24, 9 February 2016

2016-02-09T17:24:29Z

←Older revision		Revision as of 17:24, 9 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=1kfk ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:29, 11 September 2015

2015-09-11T00:29:23Z

←Older revision		Revision as of 00:29, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1kfk' size='340' side='right' caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1kfk' size='340' side='right' caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kfk]] 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~~] and [http://en.wikipedia.org/wiki/~~Salmonella_enterica_subsp._enterica_serovar_typhimurium_str._lt2 Salmonella enterica subsp. enterica serovar typhimurium str. lt2~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kfk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=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">[[1bks\|1bks]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bks\|1bks]]</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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [http://www.ebi.ac.uk/pdbsum/1kfk 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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [http://pdbe.org/1kfk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [http://www.ebi.ac.uk/pdbsum/1kfk PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		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 1kfk" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Salmonella enterica subsp. enterica serovar typhimurium]]~~	+	[[Category: Salty]]
-	~~[[Category: Salmonella enterica subsp. enterica serovar typhimurium str. lt2~~]]	+
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
	[[Category: Arac, D]]		[[Category: Arac, D]]

OCA at 08:21, 25 December 2014

2014-12-25T08:21:46Z

←Older revision		Revision as of 08:21, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1kfk]] 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] and [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium_str._lt2 Salmonella enterica subsp. enterica serovar typhimurium str. lt2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFK FirstGlance]. <br>		<table><tr><td colspan='2'>[[1kfk]] 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] and [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium_str._lt2 Salmonella enterica subsp. enterica serovar typhimurium str. lt2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFK FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=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">[[1bks\|1bks]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bks\|1bks]]</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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [http://www.ebi.ac.uk/pdbsum/1kfk 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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [http://www.ebi.ac.uk/pdbsum/1kfk 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]]
Line 36:		Line 38:
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium str. lt2]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium str. lt2]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
-	[[Category: Arac, D.]]	+	[[Category: Arac, D]]
-	[[Category: Dunn, M F.]]	+	[[Category: Dunn, M F]]
-	[[Category: Kulik, V.]]	+	[[Category: Kulik, V]]
-	[[Category: Niks, D.]]	+	[[Category: Niks, D]]
-	[[Category: Schlichting, I.]]	+	[[Category: Schlichting, I]]
-	[[Category: Seidel, R.]]	+	[[Category: Seidel, R]]
-	[[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]]

OCA at 10:27, 28 September 2014

2014-09-28T10:27:35Z

←Older revision		Revision as of 10:27, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1kfk.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of Tryptophan Synthase From Salmonella Typhimurium==
		+	<StructureSection load='1kfk' size='340' side='right' caption='[[1kfk]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1kfk]] 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] and [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium_str._lt2 Salmonella enterica subsp. enterica serovar typhimurium str. lt2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFK FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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">[[1bks\|1bks]]</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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [http://www.ebi.ac.uk/pdbsum/1kfk 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/kf/1kfk_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The catalytic activity and substrate channeling of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is regulated by allosteric interactions that modulate the switching of the enzyme between open, low activity and closed, high activity states during the catalytic cycle. The highly conserved alphaThr183 residue is part of loop alphaL6 and is located next to the alpha-active site and forms part of the alpha-beta subunit interface. The role of the interactions of alphaThr183 in alpha-site catalysis and allosteric regulation was investigated by analyzing the kinetics and crystal structures of the isosteric mutant alphaThr183Val. The mutant displays strongly impaired allosteric alpha-beta communication, and the catalytic activity of the alpha-reaction is reduced one hundred fold, whereas the beta-activity is not affected. The structural work establishes that the basis for the missing inter-subunit signaling is the lack of loop alphaL6 closure even in the presence of the alpha-subunit ligands, 3-indolyl-D-glycerol 3'-phosphate, or 3-indolylpropanol 3'-phosphate. The structural basis for the reduced alpha-activity has its origins in the missing hydrogen bond between alphaThr183 and the catalytic residue, alphaAsp60.

-	~~{{STRUCTURE_1kfk\| PDB=1kfk \| SCENE= }}~~	+	On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase.,Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I J Mol Biol. 2002 Dec 6;324(4):677-90. PMID:12460570<ref>PMID:12460570</ref>

-	~~===Crystal structure of Tryptophan Synthase~~ From ~~Salmonella Typhimurium===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_12460570}}~~	+	==See Also==
-		+	*[[Tryptophan synthase\|Tryptophan synthase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1kfk~~]] 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=1KFK OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:012460570<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
		+	[[Category: Salmonella enterica subsp. enterica serovar typhimurium str. lt2]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
	[[Category: Arac, D.]]		[[Category: Arac, D.]]

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

2012-12-05T20:11:52Z

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

←Older revision

Revision as of 20:11, 5 December 2012

OCA at 20:11, 5 December 2012

2012-12-05T20:11:49Z

←Older revision		Revision as of 20:11, 5 December 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1kfk.png\|left\|200px]]		[[Image:1kfk.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1kfk", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1kfk\| PDB=1kfk \| SCENE= }}		{{STRUCTURE_1kfk\| PDB=1kfk \| SCENE= }}

	===Crystal structure of Tryptophan Synthase From Salmonella Typhimurium===		===Crystal structure of Tryptophan Synthase From Salmonella Typhimurium===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12460570}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12460570 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_12460570}}		{{ABSTRACT_PUBMED_12460570}}

	==About this Structure==		==About this Structure==
-	~~1KFK~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/~~Salmonella_typhimurium~~ Salmonella ~~typhimurium] and [http://en~~.~~wikipedia.org/wiki/Salmonella_typhimurium_lt2 Salmonella~~ typhimurium ~~lt2~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA].	+	[[1kfk]] 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=1KFK OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12460570~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012460570</ref><references group="xtra"/>
-	[[Category: Salmonella typhimurium]]	+	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
-	~~[[Category: Salmonella typhimurium lt2~~]]	+
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
	[[Category: Arac, D.]]		[[Category: Arac, D.]]
Line 35:		Line 22:
	[[Category: Weyand, M.]]		[[Category: Weyand, M.]]
	[[Category: Carbon-oxygen lyase]]		[[Category: Carbon-oxygen lyase]]
		+	[[Category: Lyase]]
	[[Category: Pyridoxal phosphate]]		[[Category: Pyridoxal phosphate]]
	[[Category: Tryptophan biosynthesis]]		[[Category: Tryptophan biosynthesis]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:30:28 2009''