1flj: Difference between revisions
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==CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III== | ==CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III== | ||
<StructureSection load='1flj' size='340' side='right' caption='[[1flj]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1flj' size='340' side='right' caption='[[1flj]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=1flj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flj OCA], [http://pdbe.org/1flj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1flj RCSB], [http://www.ebi.ac.uk/pdbsum/1flj 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=1flj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flj OCA], [http://pdbe.org/1flj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1flj RCSB], [http://www.ebi.ac.uk/pdbsum/1flj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1flj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1flj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 13:48, 13 September 2017
CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE IIICRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III
Structural highlights
Function[CAH3_RAT] Reversible hydration of carbon dioxide. A major participant in the liver response to oxidative stress. 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 PubMedS-Glutathiolation of carbonic anhydrase III (CAIII) occurs rapidly in hepatocytes under oxidative stress. The crystal structure of the S-glutathiolated CAIII from rat liver reveals covalent adducts on cysteines 183 and 188. Electrostatic charge and steric contacts at each modification site inversely correlate with the relative rates of reactivity of these cysteines toward glutathione (GSH). Diffuse electron density associated with the GSH adducts suggests a lack of preferred bonding interactions between CAIII and the glutathionyl moieties. Hence, the GSH adducts are available for binding by a protein capable of reducing this mixed disulfide. These properties are consistent with the participation of CAIII in the protection/recovery from the damaging effects of oxidative agents. Crystal structure of S-glutathiolated carbonic anhydrase III.,Mallis RJ, Poland BW, Chatterjee TK, Fisher RA, Darmawan S, Honzatko RB, Thomas JA FEBS Lett. 2000 Oct 6;482(3):237-41. PMID:11024467[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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