Keywords: Bovinae, Disulfide, Ligand, Lysine, Pancreatic Ribonuclease, Solvent, Animal, Article, Cattle, Chemical Structure, Chemistry, Crystallization, Enzyme Active Site, Metabolism, Protein Conformation, Protein Folding, X Ray Crystallography, Catalytic Domain, X-Ray, Hydrogen-Ion Concentration, Models, Molecular,
Affiliations: *** IBB - CNR ***
Dipartimento di Chimica, Univ. degli Studi Napoli Federico II, Complesso Univ. Monte Sant' Angelo, Via Cinthia, 1-80126 Napoli, Italy
References: Not available.
Atomic resolution structures of ribonuclease A at six pH values
The diffraction pattern of protein crystals extending to atomic resolution guarantees a very accurate picture of the molecular structure and enables the study of subtle phenomena related to protein functionality. Six structures of bovine pancreatic ribonuclease at the pH* values 5.2, 5.9, 6.3, 7.1, 8.0 and 8.8 and at resolution limits in the range 1.05-1.15 Å have been refined. An overall description of the six structures and several aspects, mainly regarding pH-triggered conformational changes, are described here. Since subtle variations were expected, a thorough validation assessment of the six refined models was first carried out. Some stereochemical parameters, such as the N-Cα-C angle and the pyramidalization at the carbonyl C atoms, indicate that the standard target values and their weights typically used in refinement may need revision. A detailed comparison of the six structures has provided experimental evidence on the role of Lys41 in catalysis. Furthermore, insights are given into the structural effects related to the pH-dependent binding of a sulfate anion, which mimics the phosphate group of RNA, in the active site. Finally, the results support a number of thermodynamic and kinetic experimental data concerning the role of the disulfide bridge between Cys65 and Cys72 in the folding of RNase A.
Atomic resolution structures of ribonuclease A at six pH values
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