1v7y: Difference between revisions
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<StructureSection load='1v7y' size='340' side='right'caption='[[1v7y]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1v7y' size='340' side='right'caption='[[1v7y]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1v7y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1v7y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V7Y 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]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1v7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7y OCA], [https://pdbe.org/1v7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v7y RCSB], [https://www.ebi.ac.uk/pdbsum/1v7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v7y ProSAT], [https://www.topsan.org/Proteins/RSGI/1v7y TOPSAN]</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=1v7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7y OCA], [https://pdbe.org/1v7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v7y RCSB], [https://www.ebi.ac.uk/pdbsum/1v7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v7y ProSAT], [https://www.topsan.org/Proteins/RSGI/1v7y TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TRPA_ECOLI TRPA_ECOLI] 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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ishizuka M]] | |||
[[Category: Ishizuka | [[Category: Morimoto Y]] | ||
[[Category: Morimoto | [[Category: Nishio K]] | ||
[[Category: Nishio | [[Category: Ogasahara K]] | ||
[[Category: Ogasahara | [[Category: Tsukihara T]] | ||
[[Category: Yutani K]] | |||
[[Category: Tsukihara | |||
[[Category: Yutani | |||
Latest revision as of 02:59, 28 December 2023
Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperatureCrystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature
Structural highlights
FunctionTRPA_ECOLI 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 PubMedWhen the tryptophan synthase alpha- and beta(2)-subunits combine to form the alpha(2)beta(2)-complex, the enzymatic activity of each subunit is stimulated by 1-2 orders of magnitude. To elucidate the structural basis of this mutual activation, it is necessary to determine the structures of the alpha- and beta-subunits alone and together with the alpha(2)beta(2)-complex. The crystal structures of the tryptophan synthase alpha(2)beta(2)-complex from Salmonella typhimurium (Stalpha(2)beta(2)-complex) have already been reported. However, the structures of the subunit alone from mesophiles have not yet been determined. The structure of the tryptophan synthase alpha-subunit alone from Escherichia coli (Ecalpha-subunit) was determined by an X-ray crystallographic analysis at 2.3 A, which is the first report on the subunits alone from the mesophiles. The biggest difference between the structures of the Ecalpha-subunit alone and the alpha-subunit in the Stalpha(2)beta(2)-complex (Stalpha-subunit) was as follows. Helix 2' in the Stalpha-subunit, including an active site residue (Asp60), was changed to a flexible loop in the Ecalpha-subunit alone. The conversion of the helix to a loop resulted in the collapse of the correct active site conformation. This region is also an important part for the mutual activation in the Stalpha(2)beta(2)-complex and interaction with the beta-subunit. These results suggest that the formation of helix 2'that is essential for the stimulation of the enzymatic activity of the alpha-subunit is constructed by the induced-fit mode involved in conformational changes upon interaction between the alpha- and beta-subunits. This also confirms the prediction of the conformational changes based on the thermodynamic analysis for the association between the alpha- and beta-subunits. Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone.,Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K Biochemistry. 2005 Feb 1;44(4):1184-92. PMID:15667212[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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