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<StructureSection load='2dxb' size='340' side='right'caption='[[2dxb]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='2dxb' size='340' side='right'caption='[[2dxb]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2dxb]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_thiocyanoxidans"_happold_and_key_1937 "bacterium thiocyanoxidans" happold and key 1937]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DXB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DXB FirstGlance]. <br>
<table><tr><td colspan='2'>[[2dxb]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_thiocyanoxidans"_happold_and_key_1937 "bacterium thiocyanoxidans" happold and key 1937]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DXB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3CO:COBALT+(III)+ION'>3CO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dxc|2dxc]], [[2dd5|2dd5]], [[2dd4|2dd4]]</div></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'>[https://en.wikipedia.org/wiki/Thiocyanate_hydrolase Thiocyanate hydrolase], with EC number [https://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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dxb 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=2dxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dxb OCA], [https://pdbe.org/2dxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dxb RCSB], [https://www.ebi.ac.uk/pdbsum/2dxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dxb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SCNA_THITI SCNA_THITI]] Involved in the degradation of thiocyanate. [[http://www.uniprot.org/uniprot/SCNC_THITI SCNC_THITI]] Involved in the degradation of thiocyanate. [[http://www.uniprot.org/uniprot/SCNB_THITI SCNB_THITI]] Involved in the degradation of thiocyanate.  
[[https://www.uniprot.org/uniprot/SCNA_THITI SCNA_THITI]] Involved in the degradation of thiocyanate. [[https://www.uniprot.org/uniprot/SCNC_THITI SCNC_THITI]] Involved in the degradation of thiocyanate. [[https://www.uniprot.org/uniprot/SCNB_THITI SCNB_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]]

Revision as of 20:18, 15 December 2021

Recombinant thiocyanate hydrolase comprising partially-modified cobalt centersRecombinant thiocyanate hydrolase comprising partially-modified cobalt centers

Structural highlights

2dxb is a 24 chain structure with sequence from "bacterium_thiocyanoxidans"_happold_and_key_1937 "bacterium thiocyanoxidans" happold and key 1937. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:,
Activity:Thiocyanate hydrolase, with EC number 3.5.5.8
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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.

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

  1. ↑ Arakawa T, Kawano Y, Katayama Y, Nakayama H, Dohmae N, Yohda M, Odaka M. Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification. J Am Chem Soc. 2009 Sep 28. PMID:19785438 doi:10.1021/ja903979s

2dxb, resolution 2.25Å

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