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| | <StructureSection load='6oso' size='340' side='right'caption='[[6oso]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6oso' size='340' side='right'caption='[[6oso]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6oso]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OSO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OSO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6oso]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OSO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ouy|6ouy]], [[5n2p|5n2p]], [[5kmy|5kmy]], [[3vnd|3vnd]], [[3tha|3tha]], [[2ekc|2ekc]], [[2dzp|2dzp]], [[1v7y|1v7y]], [[1wq5|1wq5]], [[1xc4|1xc4]], [[1xcf|1xcf]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpA, STM1727 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</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=6oso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oso OCA], [https://pdbe.org/6oso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oso RCSB], [https://www.ebi.ac.uk/pdbsum/6oso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oso ProSAT]</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://proteopedia.org/fgij/fg.htm?mol=6oso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oso OCA], [http://pdbe.org/6oso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oso RCSB], [http://www.ebi.ac.uk/pdbsum/6oso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oso 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. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Tryptophan synthase]]
| + | [[Category: Chang C]] |
| - | [[Category: Chang, C]] | + | [[Category: Dunn MF]] |
| - | [[Category: Dunn, M F]] | + | [[Category: Fan L]] |
| - | [[Category: Fan, L]] | + | [[Category: Hilario E]] |
| - | [[Category: Hilario, E]] | + | [[Category: Mueller L]] |
| - | [[Category: Mueller, L]] | + | |
| - | [[Category: Alpha-chain]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Recombinant protein]]
| + | |
| - | [[Category: Wild-type]]
| + | |
| Structural highlights
Function
TRPA_SALTY The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Publication Abstract from PubMed
Backbone assignments for the isolated alpha-subunit of Salmonella typhimurium tryptophan synthase (TS) are reported based on triple resonance solution-state NMR experiments on a uniformly (2)H,(13)C,(15)N-labeled sample. From the backbone chemical shifts, secondary structure and random coil index order parameters (RCI-S(2)) are predicted. Titration with the 3-indole-D-glycerol 3'-phosphate analog, N-(4'-trifluoromethoxybenzenesulfonyl)-2-aminoethyl phosphate (F9), leads to chemical shift perturbations indicative of conformational changes from which an estimate of the dissociation constant is obtained. Comparisons of the backbone chemical-shifts, RCI-S(2) values, and site-specific relaxation times with and without F9 reveal allosteric changes including modulation in secondary structures and loop rigidity induced upon ligand binding. A comparison is made to the X-ray crystal structure of the alpha-subunit in the full TS alphabetabetaalpha bi-enzyme complex and to two new X-ray crystal structures of the isolated TS alpha-subunit reported in this work.
Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase alpha-subunit from solution-state NMR.,Sakhrani VV, Hilario E, Caulkins BG, Hatcher-Skeers ME, Fan L, Dunn MF, Mueller LJ J Biomol NMR. 2020 Jul;74(6-7):341-354. doi: 10.1007/s10858-020-00320-2. Epub, 2020 May 15. PMID:32415580[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sakhrani VV, Hilario E, Caulkins BG, Hatcher-Skeers ME, Fan L, Dunn MF, Mueller LJ. Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase alpha-subunit from solution-state NMR. J Biomol NMR. 2020 Jul;74(6-7):341-354. doi: 10.1007/s10858-020-00320-2. Epub, 2020 May 15. PMID:32415580 doi:http://dx.doi.org/10.1007/s10858-020-00320-2
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