2dxb: Difference between revisions
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==Recombinant thiocyanate hydrolase comprising partially-modified cobalt centers== | ==Recombinant thiocyanate hydrolase comprising partially-modified cobalt centers== | ||
<StructureSection load='2dxb' size='340' side='right' caption='[[2dxb]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='2dxb' size='340' side='right' caption='[[2dxb]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dxc|2dxc]], [[2dd5|2dd5]], [[2dd4|2dd4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dxc|2dxc]], [[2dd5|2dd5]], [[2dd4|2dd4]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dxb OCA], [http://pdbe.org/2dxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dxb RCSB], [http://www.ebi.ac.uk/pdbsum/2dxb PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dxb OCA], [http://pdbe.org/2dxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dxb RCSB], [http://www.ebi.ac.uk/pdbsum/2dxb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dxb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dx/2dxb_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dx/2dxb_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 09:49, 6 June 2018
Recombinant thiocyanate hydrolase comprising partially-modified cobalt centersRecombinant thiocyanate hydrolase comprising partially-modified cobalt centers
Structural highlights
Function[SCNA_THITI] Involved in the degradation of thiocyanate. [SCNC_THITI] Involved in the degradation of thiocyanate. [SCNB_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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bacterium thiocyanoxidans happold and key 1937
- Thiocyanate hydrolase
- Arakawa, T
- Katayama, Y
- Kawano, Y
- Odaka, M
- Yohda, M
- Carbonyl sulfide
- Claw setting
- Cobalt
- Complex
- Enzyme
- Hydrolase
- Metalloprotein
- Model complex
- Nitrile hydratase
- Non-corrin
- Post-translational modification
- Protein
- Sulfenate
- Sulfenic acid
- Sulfinate
- Sulfinic acid
- Thiocyanate