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1oas
From Proteopedia
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| - | [[Image:1oas.png|left|200px]] | ||
| - | + | ==O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM== | |
| + | <StructureSection load='1oas' size='340' side='right'caption='[[1oas]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1oas]] 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=1OAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAS 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]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1oas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oas OCA], [https://pdbe.org/1oas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oas RCSB], [https://www.ebi.ac.uk/pdbsum/1oas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oas ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CYSK_SALTY CYSK_SALTY] Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | ||
| + | == 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/oa/1oas_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=1oas ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The last step in cysteine biosynthesis in enteric bacteria is catalyzed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase. Here we report the crystal structure at 2.2 A resolution of the A-isozyme of O-acetylserine sulfhydrylase isolated from Salmonella typhimurium. O-acetylserine sulfhydrylase shares the same fold with tryptophan synthase-beta from Salmonella typhimurium but the sequence identity level is below 20%. There are some major structural differences: the loops providing the interface to the alpha-subunit in tryptophan synthase-beta and two surface helices of tryptophan synthase-beta are missing in O-acetylserine sulfhydrylase. The hydrophobic channel for indole transport from the alpha to the beta active site of tryptophan synthase-beta is, not unexpectedly, also absent in O-acetylserine sulfhydrylase. The dimer interface, on the other hand, is more or less conserved in the two enzymes. The active site cleft of O-acetylserine sulfhydrylase is wider and therefore more exposed to the solvent. A possible binding site for the substrate O-acetylserine is discussed. | ||
| - | + | Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium.,Burkhard P, Rao GS, Hohenester E, Schnackerz KD, Cook PF, Jansonius JN J Mol Biol. 1998;283(1):121-33. PMID:9761678<ref>PMID:9761678</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1oas" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Salmonella enterica subsp. enterica serovar | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Burkhard | + | [[Category: Burkhard P]] |
| - | [[Category: Cook | + | [[Category: Cook PF]] |
| - | [[Category: Hohenester | + | [[Category: Hohenester E]] |
| - | [[Category: Jansonius | + | [[Category: Jansonius JN]] |
| - | [[Category: Rao | + | [[Category: Rao GSJ]] |
| - | [[Category: Schnackerz | + | [[Category: Schnackerz KD]] |
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Current revision
O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM
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