2dxc: Difference between revisions

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-[[Image:2dxc.jpg|left|200px]]
- {{Structure
+==Recombinant thiocyanate hydrolase, fully-matured form==
-|PDB= 2dxc |SIZE=350|CAPTION= <scene name='initialview01'>2dxc</scene>, resolution 1.90&Aring;
+<StructureSection load='2dxc' size='340' side='right'caption='[[2dxc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=3CO:COBALT+(III)+ION'>3CO</scene> and <scene name='pdbligand=TLA:L(+)-TARTARIC ACID'>TLA</scene>
+<table><tr><td colspan='2'>[[2dxc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thiobacillus_thioparus Thiobacillus thioparus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DXC FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Thiocyanate_hydrolase Thiocyanate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.5.8 3.5.5.8]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3CO:COBALT+(III)+ION'>3CO</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=2dxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dxc OCA], [https://pdbe.org/2dxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dxc RCSB], [https://www.ebi.ac.uk/pdbsum/2dxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dxc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SCNA_THITI SCNA_THITI] Involved in the degradation of thiocyanate.
+== 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/dx/2dxc_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=2dxc ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Thiocyanate hydrolase (SCNase) is a member of a family of nitrile hydratase proteins, each of which contains a unique noncorrin cobalt center with two post-translationally modified cysteine ligands, cysteine-sulfenic acid or -sulfenate (Cys-SO(H)), and cysteine-sulfininate (Cys-SO(2)(-)), respectively. We have found that a partially matured recombinant SCNase was activated during storage. The crystal structures of SCNase before and after storage demonstrated that Cys-SO(2)(-) modification of gammaCys131 proceeded to completion prior to storage, while Cys-SO(H) modification of gammaCys133 occurred during storage. SCNase activity was suppressed when gammaCys133 was further oxidized to Cys-SO(2)(-). The correlation between the catalytic activity and the extent of the gammaCys133 modification indicates that the cysteine sulfenic acid modification of gammaCys133 is of primary importance in determining the activity of SCNase.
-'''Recombinant thiocyanate hydrolase, fully-matured form'''
+Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification.,Arakawa T, Kawano Y, Katayama Y, Nakayama H, Dohmae N, Yohda M, Odaka M J Am Chem Soc. 2009 Sep 28. PMID:19785438<ref>PMID:19785438</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-DXC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thiobacillus_thioparus Thiobacillus thioparus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DXC OCA].
+<div class="pdbe-citations 2dxc" style="background-color:#fffaf0;"></div>
-[[Category: Protein complex]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Thiobacillus thioparus]]
-[[Category: Thiocyanate hydrolase]]
+[[Category: Arakawa T]]
-[[Category: Arakawa, T.]]
+[[Category: Katayama Y]]
-[[Category: Katayama, Y.]]
+[[Category: Kawano Y]]
-[[Category: Kawano, Y.]]
+[[Category: Odaka M]]
-[[Category: Odaka, M.]]
+[[Category: Yohda M]]
-[[Category: Yohda, M.]]
-[[Category: 3CO]]
-[[Category: TLA]]
-[[Category: carbonyl sulfide]]
-[[Category: claw setting]]
-[[Category: cobalt]]
-[[Category: complex]]
-[[Category: enzyme]]
-[[Category: hydrolase]]
-[[Category: metalloprotein]]
-[[Category: model complex]]
-[[Category: nitrile hydratase]]
-[[Category: non-corrin]]
-[[Category: post-translational modification]]
-[[Category: protein]]
-[[Category: sulfenate]]
-[[Category: sulfenic acid]]
-[[Category: sulfinate]]
-[[Category: sulfinic acid]]
-[[Category: thiocyanate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:32:46 2008''