2dxb
From Proteopedia
(Difference between revisions)
| (20 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2dxb.jpg|left|200px]]<br /><applet load="2dxb" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2dxb, resolution 2.25Å" /> | ||
| - | '''Recombinant thiocyanate hydrolase comprising partially-modified cobalt centers'''<br /> | ||
| - | == | + | ==Recombinant thiocyanate hydrolase comprising partially-modified cobalt centers== |
| - | + | <StructureSection load='2dxb' size='340' side='right'caption='[[2dxb]], [[Resolution|resolution]] 2.25Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[2dxb]] is a 24 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</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=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=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> |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/SCNA_THITI SCNA_THITI] Involved in the degradation of thiocyanate. |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <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/initialview03.spt</scriptWhenUnchecked> | |
| - | [ | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [[ | + | </jmolCheckbox> |
| - | [ | + | </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=2dxb ConSurf]. |
| - | + | <div style="clear:both"></div> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == 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<ref>PMID:19785438</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2dxb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thiobacillus thioparus]] | ||
| + | [[Category: Arakawa T]] | ||
| + | [[Category: Katayama Y]] | ||
| + | [[Category: Kawano Y]] | ||
| + | [[Category: Odaka M]] | ||
| + | [[Category: Yohda M]] | ||
Current revision
Recombinant thiocyanate hydrolase comprising partially-modified cobalt centers
| |||||||||||
