1kfj: Difference between revisions
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<StructureSection load='1kfj' size='340' side='right'caption='[[1kfj]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1kfj' size='340' side='right'caption='[[1kfj]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kfj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1kfj]] 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=1KFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFJ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <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=PLS:[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-SERINE'>PLS</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=1kfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfj OCA], [https://pdbe.org/1kfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfj RCSB], [https://www.ebi.ac.uk/pdbsum/1kfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfj 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=1kfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfj OCA], [https://pdbe.org/1kfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfj RCSB], [https://www.ebi.ac.uk/pdbsum/1kfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfj 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] | ||
[[Category: Arac | [[Category: Arac D]] | ||
[[Category: Dunn | [[Category: Dunn MF]] | ||
[[Category: Kulik | [[Category: Kulik V]] | ||
[[Category: Niks | [[Category: Niks D]] | ||
[[Category: Schlichting | [[Category: Schlichting I]] | ||
[[Category: Seidel | [[Category: Seidel R]] | ||
[[Category: Weyand | [[Category: Weyand M]] | ||
Latest revision as of 11:57, 16 August 2023
CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH L-SERINECRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH L-SERINE
Structural highlights
FunctionTRPA_SALTY The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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