Crystal structure of S-glutathiolated carbonic anhydrase III

Robert J. Mallis, Bradley W. Poland, Tapan K. Chatterjee, Rory A. Fisher, Steven Darmawan, Richard B. Honzatko, James A. Thomas

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

Abstract

S-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. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)237-241
Number of pages5
JournalFEBS Letters
Volume482
Issue number3
DOIs
StatePublished - Oct 6 2000

Keywords

  • Carbonic anhydrase
  • Oxidative stress
  • Protein oxidation
  • Rat liver
  • S-Glutathiolation
  • Sulfhydryl reactivity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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