PDBsum entry 1flj

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Lyase PDB id
Protein chain
260 a.a. *
GSH ×2
Waters ×216
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystal structure of s-Glutathiolated carbonic anhydrase III.
Authors R.J.Mallis, B.W.Poland, T.K.Chatterjee, R.A.Fisher, S.Darmawan, R.B.Honzatko, J.A.Thomas.
Ref. FEBS Lett, 2000, 482, 237-241. [DOI no: 10.1016/S0014-5793(00)02022-6]
PubMed id 11024467
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.
Figure 4.
Fig. 4. Stereo, surface representation of S-glutathiolated CAIII in the vicinity of the Cys183 adduct. The two conformers of the Cys183 adduct are represented by wireframe models. The disulfide bonds between GSH1 and Cys183 are shown as thin black lines. The view is approximately the same as that in Fig. 3B. The image was generated using MolMol [28]. A: Conformation 1 of the Cys183–GSH1 adduct. This is the same conformation of Cys183 as is found in the reduced bovine CAIII structure [27]. B: Conformation 2 of Cys183–GSH1 adduct.
Figure 5.
Fig. 5. Electrostatic and solvent-accessible surface representation of CAIII in stereo. Dark gray coloration represents a positive charge, light gray a negative charge and white a neutral charge. The position of S^γ of the GSH adducts are indicated by white balls. The lower portion of the figure shows the electrostatic surface of CAIII when the cysteines are in conformation 1. This is the same conformation as that of the reduced bovine CAIII model [21]. The upper portion of the figure shows the surface when Cys183 is in conformation 2. The electrostatic and surface calculations were carried out using MolMol [28], which utilizes the algorithm of Nicholls and Honig [29].
The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2000, 482, 237-241) copyright 2000.
Secondary reference #1
Title Protein sulfhydryls and their role in the antioxidant function of protein s-Thiolation.
Authors J.A.Thomas, B.Poland, R.Honzatko.
Ref. Arch Biochem Biophys, 1995, 319, 1-9.
PubMed id 7771771
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