View source for 1oas


==O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM==
<StructureSection load='1oas' size='340' side='right'caption='[[1oas]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oas]] is a 2 chain structure. 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='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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </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=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].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1oas" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cysteine synthase]]
[[Category: Large Structures]]
[[Category: Burkhard, P]]
[[Category: Cook, P F]]
[[Category: Hohenester, E]]
[[Category: Jansonius, J N]]
[[Category: Rao, G S.J]]
[[Category: Schnackerz, K D]]
[[Category: Beta replacement enzyme]]
[[Category: Cystein biosynthesis]]
[[Category: Homodimer]]
[[Category: Lyase]]
[[Category: Plp dependent enzyme]]