2dd4

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(New page: 200px<br /><applet load="2dd4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dd4, resolution 2.06&Aring;" /> '''Thiocyanate hydrolas...)
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[[Image:2dd4.jpg|left|200px]]<br /><applet load="2dd4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2dd4, resolution 2.06&Aring;" />
 
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'''Thiocyanate hydrolase (SCNase) from Thiobacillus thioparus recombinant apo-enzyme'''<br />
 
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==Overview==
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==Thiocyanate hydrolase (SCNase) from Thiobacillus thioparus recombinant apo-enzyme==
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Thiocyanate hydrolase (SCNase) of Thiobacillus thioparus THI115 is a, cobalt(III)-containing enzyme catalyzing the degradation of thiocyanate to, carbonyl sulfide and ammonia. We determined the crystal structures of the, apo- and native SCNases at a resolution of 2.0 A. SCNases in both forms, had a conserved hetero-dodecameric structure, (alphabetagamma)(4). Four, alphabetagamma hetero-trimers were structurally equivalent. One, alphabetagamma hetero-trimer was composed of the core domain and the betaN, domain, which was located at the center of the molecule and linked the, hetero-trimers with novel quaternary interfaces. In both the apo- and, native SCNases, the core domain was structurally conserved between those, of iron and cobalt-types of nitrile hydratase (NHase). Native SCNase, possessed the post-translationally modified cysteine ligands, gammaCys131-SO(2)H and gammaCys133-SOH like NHases. However, the low-spin, cobalt(III) was found to be in the distorted square-pyramidal geometry, which had not been reported before in any protein. The size as well as the, electrostatic properties of the substrate-binding pocket was totally, different from NHases with respect to the charge distribution and the, substrate accessibility, which rationally explains the differences in the, substrate preference between SCNase and NHase.
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<StructureSection load='2dd4' size='340' side='right'caption='[[2dd4]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2dd4]] 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=2DD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DD4 FirstGlance]. <br>
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2DD4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thiobacillus_thioparus Thiobacillus thioparus] with FRU and TAR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DD4 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dd4 OCA], [https://pdbe.org/2dd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dd4 RCSB], [https://www.ebi.ac.uk/pdbsum/2dd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dd4 ProSAT]</span></td></tr>
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Structure of thiocyanate hydrolase: a new nitrile hydratase family protein with a novel five-coordinate cobalt(III) center., Arakawa T, Kawano Y, Kataoka S, Katayama Y, Kamiya N, Yohda M, Odaka M, J Mol Biol. 2007 Mar 9;366(5):1497-509. Epub 2006 Dec 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17222425 17222425]
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</table>
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[[Category: Protein complex]]
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== Function ==
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[https://www.uniprot.org/uniprot/SCNA_THITI SCNA_THITI] Involved in the degradation of thiocyanate.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dd/2dd4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2dd4 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thiobacillus thioparus]]
[[Category: Thiobacillus thioparus]]
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[[Category: Thiocyanate hydrolase]]
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[[Category: Arakawa T]]
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[[Category: Arakawa, T.]]
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[[Category: Kamiya N]]
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[[Category: Kamiya, N.]]
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[[Category: Kataoka S]]
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[[Category: Kataoka, S.]]
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[[Category: Katayama Y]]
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[[Category: Katayama, Y.]]
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[[Category: Kawano Y]]
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[[Category: Kawano, Y.]]
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[[Category: Odaka M]]
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[[Category: Odaka, M.]]
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[[Category: Yohda M]]
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[[Category: Yohda, M.]]
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[[Category: FRU]]
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[[Category: TAR]]
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[[Category: carbonyl sulfide]]
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[[Category: claw setting]]
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[[Category: cobalt]]
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[[Category: complex]]
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[[Category: enzyme]]
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[[Category: hydrolase]]
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[[Category: metalloprotein]]
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[[Category: model complex]]
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[[Category: nitrile hydratase]]
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[[Category: non-corrin]]
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[[Category: protein]]
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[[Category: sulfenic acid]]
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[[Category: sulfinic acid]]
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[[Category: thiocyanate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:32:40 2007''
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Current revision

Thiocyanate hydrolase (SCNase) from Thiobacillus thioparus recombinant apo-enzyme

PDB ID 2dd4

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