2zzd: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zzd]] is a 12 chain structure with sequence 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=2ZZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZZD FirstGlance]. <br> | <table><tr><td colspan='2'>[[2zzd]] is a 12 chain structure with sequence 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=2ZZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZZD FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3CO:COBALT+(III)+ION'>3CO</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>< | </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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</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></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dd4|2dd4]], [[2dd5|2dd5]], [[2dxb|2dxb]], [[2dxc|2dxc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dd4|2dd4]], [[2dd5|2dd5]], [[2dxb|2dxb]], [[2dxc|2dxc]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">scnA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=931 Thiobacillus thioparus]), scnB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=931 Thiobacillus thioparus]), scnC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=931 Thiobacillus thioparus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">scnA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=931 Thiobacillus thioparus]), scnB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=931 Thiobacillus thioparus]), scnC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=931 Thiobacillus thioparus])</td></tr> | ||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zzd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zzd RCSB], [http://www.ebi.ac.uk/pdbsum/2zzd 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=2zzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zzd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zzd RCSB], [http://www.ebi.ac.uk/pdbsum/2zzd PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Thiobacillus thioparus]] | [[Category: Thiobacillus thioparus]] | ||
[[Category: Thiocyanate hydrolase]] | [[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: Air inactivation]] | [[Category: Air inactivation]] | ||
[[Category: Autocatalytic activation]] | [[Category: Autocatalytic activation]] | ||
Revision as of 19:24, 25 December 2014
Recombinant thiocyanate hydrolase, air-oxidized form of holo-enzymeRecombinant thiocyanate hydrolase, air-oxidized form of holo-enzyme
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?)
OCACategories:
- Thiobacillus thioparus
- Thiocyanate hydrolase
- Arakawa, T
- Katayama, Y
- Kawano, Y
- Odaka, M
- Yohda, M
- Air inactivation
- Autocatalytic activation
- Carbonyl sulfide
- Claw setting
- Cobalt
- Complex
- Cysteine
- Enzyme
- Hydrolase
- Metal-binding
- Metalloprotein
- Model complex
- Nitrile hydratase
- Non-corrin
- Oxidation
- Post-translational modification
- Protein
- Scnase
- Sulfenate
- Sulfenic acid
- Sulfinate
- Sulfinic acid
- Thiocyanate