1FLJ

CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

Summary for 1FLJ

• Entry DOI: 10.2210/pdb1flj/pdb
• Descriptor: CARBONIC ANHYDRASE III, ZINC ION, GLUTATHIONE, ... (4 entities in total)
• Functional Keywords: carbonic anhydrase iii, glutathione, s-glutathiolated, s-glutathionylated, lyase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P14141
• Total number of polymer chains: 1
• Total formula weight: 30049.33

Authors

Mallis, R.J.,Poland, B.W.,Chatterjee, T.K.,Fisher, R.A.,Darmawan, S.,Honzatko, R.B.,Thomas, J.A. (deposition date: 2000-08-14, release date: 2000-09-04, Last modification date: 2025-03-26)

Primary citation

Mallis, R.J.,Poland, B.W.,Chatterjee, T.K.,Fisher, R.A.,Darmawan, S.,Honzatko, R.B.,Thomas, J.A.
Crystal structure of S-glutathiolated carbonic anhydrase III.
FEBS Lett., 482:237-241, 2000

PubMed 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.

PubMed: 11024467
DOI: 10.1016/S0014-5793(00)02022-6

Experimental method

X-RAY DIFFRACTION (1.8 Å)