2dxc: Difference between revisions
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<StructureSection load='2dxc' size='340' side='right'caption='[[2dxc]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2dxc' size='340' side='right'caption='[[2dxc]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dxc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <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> | <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> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SCNA_THITI SCNA_THITI] Involved in the degradation of thiocyanate. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thiobacillus thioparus]] | ||
[[Category: Arakawa | [[Category: Arakawa T]] | ||
[[Category: Katayama | [[Category: Katayama Y]] | ||
[[Category: Kawano | [[Category: Kawano Y]] | ||
[[Category: Odaka | [[Category: Odaka M]] | ||
[[Category: Yohda | [[Category: Yohda M]] | ||
Revision as of 11:31, 25 October 2023
Recombinant thiocyanate hydrolase, fully-matured formRecombinant thiocyanate hydrolase, fully-matured form
Structural highlights
FunctionSCNA_THITI Involved in the degradation of thiocyanate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThiocyanate 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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