Journal article
Crystal structure of S-glutathiolated carbonic anhydrase III
FEBS letters, Vol.482(3), pp.237-241
2000
DOI: 10.1016/S0014-5793(00)02022-6
PMID: 11024467
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.
Details
- Title: Subtitle
- Crystal structure of S-glutathiolated carbonic anhydrase III
- Creators
- Robert J Mallis - Department of Biochemistry, Biophysics and Molecular Biology, 1210 Molecular Biology Bldg., Iowa State University, Ames, IA 50011, USABradley W Poland - Department of Biochemistry, Biophysics and Molecular Biology, 1210 Molecular Biology Bldg., Iowa State University, Ames, IA 50011, USATapan K Chatterjee - Department of Pharmacology, University of Iowa, Iowa City, IA 52242, USARory A Fisher - Department of Pharmacology, University of Iowa, Iowa City, IA 52242, USASteven Darmawan - Department of Biochemistry, Biophysics and Molecular Biology, 1210 Molecular Biology Bldg., Iowa State University, Ames, IA 50011, USARichard B Honzatko - Department of Biochemistry, Biophysics and Molecular Biology, 1210 Molecular Biology Bldg., Iowa State University, Ames, IA 50011, USAJames A Thomas - Department of Biochemistry, Biophysics and Molecular Biology, 1210 Molecular Biology Bldg., Iowa State University, Ames, IA 50011, USA
- Resource Type
- Journal article
- Publication Details
- FEBS letters, Vol.482(3), pp.237-241
- DOI
- 10.1016/S0014-5793(00)02022-6
- PMID
- 11024467
- NLM abbreviation
- FEBS Lett
- ISSN
- 0014-5793
- eISSN
- 1873-3468
- Publisher
- Elsevier B.V
- Language
- English
- Date published
- 2000
- Academic Unit
- Iowa Neuroscience Institute; Neuroscience and Pharmacology; Internal Medicine
- Record Identifier
- 9984040310802771
Metrics
14 Record Views