1FLJ

CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

1FLJ の概要

• エントリーDOI: 10.2210/pdb1flj/pdb
• 分子名称: CARBONIC ANHYDRASE III, ZINC ION, GLUTATHIONE, ... (4 entities in total)
• 機能のキーワード: carbonic anhydrase iii, glutathione, s-glutathiolated, s-glutathionylated, lyase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm: P14141
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30049.33

構造登録者

Mallis, R.J.,Poland, B.W.,Chatterjee, T.K.,Fisher, R.A.,Darmawan, S.,Honzatko, R.B.,Thomas, J.A. (登録日: 2000-08-14, 公開日: 2000-09-04, 最終更新日: 2025-03-26)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)