1cx9: Difference between revisions

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 <StructureSection load='1cx9' size='340' side='right'caption='[[1cx9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cx9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CX9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cx9]] 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=1CX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CX9 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=NHP:4-(2-AMINOPHENYLTHIO)-BUTYLPHOSPHONIC+ACID'>NHP</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]] 2.3&#8491;</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]], [[1cw2|1cw2]]</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=NHP:4-(2-AMINOPHENYLTHIO)-BUTYLPHOSPHONIC+ACID'>NHP</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=1cx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cx9 OCA], [https://pdbe.org/1cx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cx9 RCSB], [https://www.ebi.ac.uk/pdbsum/1cx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cx9 ProSAT]</span></td></tr>
 </table>
 == 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/TRPB_SALTY TRPB_SALTY] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
 == Evolutionary Conservation ==
 [[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=1cx9 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.
-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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1cx9" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[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]]