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1flj

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1flj, resolution 1.80Å ()
Ligands: ,
Non-Standard Residues:
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1flj is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

See Also

Reference

  • Mallis RJ, Poland BW, Chatterjee TK, Fisher RA, Darmawan S, Honzatko RB, Thomas JA. Crystal structure of S-glutathiolated carbonic anhydrase III. FEBS Lett. 2000 Oct 6;482(3):237-41. PMID:11024467

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