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New page: left|200px<br /><applet load="1wkv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wkv, resolution 2.0Å" /> '''Crystal structure of ...
 
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[[Image:1wkv.gif|left|200px]]<br /><applet load="1wkv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wkv, resolution 2.0&Aring;" />
'''Crystal structure of O-phosphoserine sulfhydrylase'''<br />


==Overview==
==Crystal structure of O-phosphoserine sulfhydrylase==
O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic, archaeon, Aeropyrum pernix K1. This enzyme catalyzes a novel cysteine, synthetic reaction from O-phospho-l-serine and sulfide. The crystal, structure of the enzyme was determined at 2.0A resolution using the method, of multi-wavelength anomalous dispersion. A monomer consists of three, domains, including an N-terminal domain with a new alpha/beta fold. The, topology folds of the middle and C-terminal domains were similar to those, of the O-acetylserine sulfhydrylase-A from Salmonella typhimurium and the, cystathionine beta-synthase from human. The cofactor, pyridoxal, 5'-phosphate, is bound in a cleft between the middle and C-terminal, domains through a covalent linkage to Lys127. Based on the structure, determined, O-phospho-l-serine could be rationally modeled into the active, site of the enzyme. An enzyme-substrate complex model and a mutation, experiment revealed that Arg297, unique to hyperthermophilic archaea, is, one of the most crucial residues for O-phosphoserine sulfhydrylation, activity. There are more hydrophobic areas and less electric charges at, the dimer interface, compared to the S.typhimurium O-acetylserine, sulfhydrylase.
<StructureSection load='1wkv' size='340' side='right'caption='[[1wkv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wkv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WKV 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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=1wkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wkv OCA], [https://pdbe.org/1wkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wkv RCSB], [https://www.ebi.ac.uk/pdbsum/1wkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wkv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYSO_AERPE CYSO_AERPE] Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.<ref>PMID:12644499</ref>
== 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/wk/1wkv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1wkv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic archaeon, Aeropyrum pernix K1. This enzyme catalyzes a novel cysteine synthetic reaction from O-phospho-l-serine and sulfide. The crystal structure of the enzyme was determined at 2.0A resolution using the method of multi-wavelength anomalous dispersion. A monomer consists of three domains, including an N-terminal domain with a new alpha/beta fold. The topology folds of the middle and C-terminal domains were similar to those of the O-acetylserine sulfhydrylase-A from Salmonella typhimurium and the cystathionine beta-synthase from human. The cofactor, pyridoxal 5'-phosphate, is bound in a cleft between the middle and C-terminal domains through a covalent linkage to Lys127. Based on the structure determined, O-phospho-l-serine could be rationally modeled into the active site of the enzyme. An enzyme-substrate complex model and a mutation experiment revealed that Arg297, unique to hyperthermophilic archaea, is one of the most crucial residues for O-phosphoserine sulfhydrylation activity. There are more hydrophobic areas and less electric charges at the dimer interface, compared to the S.typhimurium O-acetylserine sulfhydrylase.


==About this Structure==
Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution.,Oda Y, Mino K, Ishikawa K, Ataka M J Mol Biol. 2005 Aug 12;351(2):334-44. PMID:16005886<ref>PMID:16005886</ref>
1WKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with ACT and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WKV OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution., Oda Y, Mino K, Ishikawa K, Ataka M, J Mol Biol. 2005 Aug 12;351(2):334-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16005886 16005886]
</div>
[[Category: Aeropyrum pernix]]
<div class="pdbe-citations 1wkv" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Ataka, M.]]
<references/>
[[Category: Ishikawa, K.]]
__TOC__
[[Category: Mino, K.]]
</StructureSection>
[[Category: Oda, Y.]]
[[Category: Aeropyrum pernix K1]]
[[Category: ACT]]
[[Category: Large Structures]]
[[Category: PLP]]
[[Category: Ataka M]]
[[Category: homodimer]]
[[Category: Ishikawa K]]
[[Category: open alpha/beta folding]]
[[Category: Mino K]]
 
[[Category: Oda Y]]
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