1cw2 - Revision history

OCA at 13:22, 13 March 2024

2024-03-13T13:22:04Z

←Older revision		Revision as of 13:22, 13 March 2024
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	<StructureSection load='1cw2' size='340' side='right'caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1cw2' size='340' side='right'caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cw2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cw2]] 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=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=HSP:4~~-(2~~-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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]] 2Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HSP:4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [https://pdbe.org/1cw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [https://www.ebi.ac.uk/pdbsum/1cw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cw2 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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [https://pdbe.org/1cw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [https://www.ebi.ac.uk/pdbsum/1cw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cw2 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=1cw2 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=1cw2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	In an effort to use a structure-based approach for the design of new herbicides, the crystal structures of complexes of tryptophan synthase with a series of phosphonate enzyme inhibitors were determined at 2.3 A or higher resolution. These inhibitors were designed to mimic the transition state formed during the alpha-reaction of the enzyme and, as expected, have affinities much greater than that of the natural substrate indole-3-glycerol phosphate or its nonhydrolyzable analogue indole propanol phosphate (IPP). These inhibitors are ortho-substituted arylthioalkylphosphonate derivatives that have an sp(3)-hybridized sulfur atom, designed to mimic the putative tetrahedral transition state at the C3 atom of the indole, and lack the C2 atom to allow for higher conformational flexibility. Overall, the inhibitors bind in a fashion similar to that of IPP. Glu-49 and Phe-212 are the two active site residues whose conformation changes upon inhibitor binding. A very short hydrogen bond between a phosphonate oxygen and the Ser-235 hydroxyl oxygen may be responsible for stabilization of the enzyme-inhibitor complexes. Implications for the mechanism of catalysis as well as directions for more potent inhibitors are discussed.
-
-	Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase.,Sachpatzidis A, Dealwis C, Lubetsky JB, Liang PH, Anderson KS, Lolis E Biochemistry. 1999 Sep 28;38(39):12665-74. PMID:10504236<ref>PMID:10504236</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1cw2" 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: Anderson~~, K S~~]]	+	[[Category: Anderson KS]]
-	[[Category: Dealwis, C]]	+	[[Category: Dealwis C]]
-	[[Category: Liang~~, P H~~]]	+	[[Category: Liang PH]]
-	[[Category: Lolis, E]]	+	[[Category: Lolis E]]
-	[[Category: Lubetsky~~, J B~~]]	+	[[Category: Lubetsky JB]]
-	[[Category: Sachpatzidis, A]]	+	[[Category: Sachpatzidis A]]
-	~~[[Category: 8-fold alpha-beta barrel]]~~	+
-	~~[[Category: Enzyme-inhibitor complex]]~~	+
-	~~[[Category: Lyase~~]]	+

OCA at 10:40, 14 July 2021

2021-07-14T10:40:54Z

←Older revision		Revision as of 10:40, 14 July 2021
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	<StructureSection load='1cw2' size='340' side='right'caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1cw2' size='340' side='right'caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cw2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cw2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSP:4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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=HSP:4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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">[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [~~http~~://pdbe.org/1cw2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1cw2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1cw2 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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [https://pdbe.org/1cw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [https://www.ebi.ac.uk/pdbsum/1cw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cw2 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 06:52, 10 October 2019

2019-10-10T06:52:41Z

←Older revision		Revision as of 06:52, 10 October 2019
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	==CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID==		==CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID==
-	<StructureSection load='1cw2' size='340' side='right' caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1cw2' size='340' side='right'caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cw2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cw2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 1cw2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1cw2" 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: Anderson, K S]]		[[Category: Anderson, K S]]

OCA at 08:32, 6 December 2017

2017-12-06T08:32:06Z

←Older revision		Revision as of 08:32, 6 December 2017
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID==		==CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID==
	<StructureSection load='1cw2' size='340' side='right' caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1cw2' size='340' side='right' caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://pdbe.org/1cw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://pdbe.org/1cw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cw2 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/cw/1cw2_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cw/1cw2_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 1cw2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1cw2" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Tryptophan synthase\|Tryptophan synthase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 23:16, 8 February 2016

2016-02-08T23:16:24Z

←Older revision		Revision as of 23:16, 8 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=1cw2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 16:18, 10 September 2015

2015-09-10T16:18:04Z

←Older revision		Revision as of 16:18, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1cw2' size='340' side='right' caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1cw2' size='340' side='right' caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cw2]] 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=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cw2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSP:4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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=HSP:4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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">[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://pdbe.org/1cw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 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 1cw2" 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: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
	[[Category: Anderson, K S]]		[[Category: Anderson, K S]]

OCA at 02:49, 25 December 2014

2014-12-25T02:49:13Z

←Older revision		Revision as of 02:49, 25 December 2014
Line 8:		Line 8:
	<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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 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 18:29, 22 December 2014

2014-12-22T18:29:29Z

←Older revision		Revision as of 18:29, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cw2]] 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=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cw2]] 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=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSP:4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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=HSP:4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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">[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 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 35:		Line 35:
	[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]		[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
	[[Category: Tryptophan synthase]]		[[Category: Tryptophan synthase]]
-	[[Category: Anderson, K S.]]	+	[[Category: Anderson, K S]]
-	[[Category: Dealwis, C.]]	+	[[Category: Dealwis, C]]
-	[[Category: Liang, P H.]]	+	[[Category: Liang, P H]]
-	[[Category: Lolis, E.]]	+	[[Category: Lolis, E]]
-	[[Category: Lubetsky, J B.]]	+	[[Category: Lubetsky, J B]]
-	[[Category: Sachpatzidis, A.]]	+	[[Category: Sachpatzidis, A]]
	[[Category: 8-fold alpha-beta barrel]]		[[Category: 8-fold alpha-beta barrel]]
	[[Category: Enzyme-inhibitor complex]]		[[Category: Enzyme-inhibitor complex]]
	[[Category: Lyase]]		[[Category: Lyase]]

OCA at 09:21, 27 August 2014

2014-08-27T09:21:44Z

←Older revision		Revision as of 09:21, 27 August 2014
Line 1:		Line 1:
-	[[~~Image:~~1cw2.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID==
		+	<StructureSection load='1cw2' size='340' side='right' caption='[[1cw2]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1cw2]] 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=1CW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CW2 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSP:4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC+ACID'>HSP</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">[[1c29\|1c29]], [[1c8v\|1c8v]], [[1c9d\|1c9d]]</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=1cw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1cw2 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/cw/1cw2_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 ==
		+	In an effort to use a structure-based approach for the design of new herbicides, the crystal structures of complexes of tryptophan synthase with a series of phosphonate enzyme inhibitors were determined at 2.3 A or higher resolution. These inhibitors were designed to mimic the transition state formed during the alpha-reaction of the enzyme and, as expected, have affinities much greater than that of the natural substrate indole-3-glycerol phosphate or its nonhydrolyzable analogue indole propanol phosphate (IPP). These inhibitors are ortho-substituted arylthioalkylphosphonate derivatives that have an sp(3)-hybridized sulfur atom, designed to mimic the putative tetrahedral transition state at the C3 atom of the indole, and lack the C2 atom to allow for higher conformational flexibility. Overall, the inhibitors bind in a fashion similar to that of IPP. Glu-49 and Phe-212 are the two active site residues whose conformation changes upon inhibitor binding. A very short hydrogen bond between a phosphonate oxygen and the Ser-235 hydroxyl oxygen may be responsible for stabilization of the enzyme-inhibitor complexes. Implications for the mechanism of catalysis as well as directions for more potent inhibitors are discussed.

-	~~{{STRUCTURE_1cw2\| PDB=1cw2 \| SCENE= }}~~	+	Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase.,Sachpatzidis A, Dealwis C, Lubetsky JB, Liang PH, Anderson KS, Lolis E Biochemistry. 1999 Sep 28;38(39):12665-74. PMID:10504236<ref>PMID:10504236</ref>

-	~~===CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_10504236}}~~	+	==See Also==
-		+	*[[Tryptophan synthase\|Tryptophan synthase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1cw2~~]] 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=1CW2 OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:010504236<~~/~~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 "1cw2" [edit=sysop:move=sysop]

2012-10-21T20:16:47Z

Protected "1cw2" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:16, 21 October 2012