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[[Image:1oas.gif|left|200px]]


{{Structure
==O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM==
|PDB= 1oas |SIZE=350|CAPTION= <scene name='initialview01'>1oas</scene>, resolution 2.200&Aring;
<StructureSection load='1oas' size='340' side='right'caption='[[1oas]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>
<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>
|ACTIVITY= [http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE=  
<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>
'''O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM'''
== 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 ==
==Overview==
[[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.
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.


==About this Structure==
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>
1OAS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAS OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/9761678 9761678]
[[Category: Cysteine synthase]]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: Burkhard, P.]]
[[Category: Cook, P F.]]
[[Category: Hohenester, E.]]
[[Category: Jansonius, J N.]]
[[Category: Rao, G S.J.]]
[[Category: Schnackerz, K D.]]
[[Category: PLP]]
[[Category: beta replacement enzyme]]
[[Category: cystein biosynthesis]]
[[Category: homodimer]]
[[Category: plp dependent enzyme]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:08:12 2008''
From MEDLINE&reg;/PubMed&reg;, 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: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Burkhard P]]
[[Category: Cook PF]]
[[Category: Hohenester E]]
[[Category: Jansonius JN]]
[[Category: Rao GSJ]]
[[Category: Schnackerz KD]]
Retrieved from "https://proteopedia.org/1oas"