1qoq: Difference between revisions

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-{{STRUCTURE_1qoq|  PDB=1qoq  |  SCENE=  }}
-===CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE GLYCEROL PHOSPHATE===
-{{ABSTRACT_PUBMED_10600108}}
-==Function==
+==CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE GLYCEROL PHOSPHATE==
-[[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.
+<StructureSection load='1qoq' size='340' side='right'caption='[[1qoq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qoq]] 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=1QOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOQ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IGP:INDOLE-3-GLYCEROL+PHOSPHATE'>IGP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qoq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qoq OCA], [https://pdbe.org/1qoq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qoq RCSB], [https://www.ebi.ac.uk/pdbsum/1qoq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qoq 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.
+== 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/qo/1qoq_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/main_output.php?pdb_ID=1qoq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We used freeze trapping to stabilize the Michaelis complex of wild-type tryptophan synthase and the alpha-subunit substrate indole-3-glycerol phosphate (IGP) and determined its structure to 1. 8 A resolution. In addition, we determined the 1.4 A resolution structure of the complex with indole-3-propanole phosphate (IPP), a noncleavable IGP analogue. The interaction of the 3'-hydroxyl of IGP with the catalytic alphaGlu49 leads to a twisting of the propane chain and to a repositioning of the indole ring compared to IPP. Concomitantly, the catalytic alphaAsp60 rotates resulting in a translocation of the COMM domain [betaGly102-betaGly189, for definition see Schneider et al. (1998) Biochemistry 37, 5394-5406] in a direction opposite to the one in the IPP complex. This results in loss of the allosteric sodium ion bound at the beta-subunit and an opening of the beta-active site, thereby making the cofactor pyridoxal 5'-phosphate (PLP) accessible to solvent and thus serine binding. These findings form the structural basis for the information transfer from the alpha- to the beta-subunit and may explain the affinity increase of the beta-active site for serine upon IGP binding.
-==About this Structure==
+Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate.,Weyand M, Schlichting I Biochemistry. 1999 Dec 14;38(50):16469-80. PMID:10600108<ref>PMID:10600108</ref>
-[[1qoq]] 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=1QOQ OCA].
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1qoq" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Tryptophan synthase|Tryptophan synthase]]
+*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:010600108</ref><references group="xtra"/><references/>
+__TOC__
-[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
+</StructureSection>
-[[Category: Tryptophan synthase]]
+[[Category: Large Structures]]
-[[Category: Schlichting, I.]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-[[Category: Weyand, M.]]
+[[Category: Schlichting I]]
-[[Category: Carbon-oxygen lyase]]
+[[Category: Weyand M]]
-[[Category: Lyase]]
-[[Category: Pyridoxal phosphate]]
-[[Category: Tryptophan biosynthesis]]