1Z3P
X-Ray crystal structure of a mutant Ribonuclease S (M13Nva)
1Z3P の概要
| エントリーDOI | 10.2210/pdb1z3p/pdb |
| 関連するPDBエントリー | 1D5D 1D5E 1D5H 1RBC 1RBD 1RBH 1Z3L 1Z3M |
| 分子名称 | Ribonuclease pancreatic, S-Peptide, Ribonuclease pancreatic, S-Protein, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | rnase s mutant (m13nva), s-peptide, s-protein, cavity, hydrolase |
| 由来する生物種 | Bos taurus (cattle) 詳細 |
| 細胞内の位置 | Secreted: P61823 P61823 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 13468.99 |
| 構造登録者 | |
| 主引用文献 | Das, M.,Rao, B.V.,Ghosh, S.,Varadarajan, R. Attempts to delineate the relative contributions of changes in hydrophobicity and packing to changes in stability of ribonuclease S mutants. Biochemistry, 44:5923-5930, 2005 Cited by PubMed Abstract: While the hydrophobic driving force is thought to be a major contributor to protein stability, it is difficult to experimentally dissect out its contribution to the overall free energy of folding. We have made large to small substitutions of buried hydrophobic residues at positions 8 and 13 in the peptide/protein complex, RNase-S, and have characterized the structures by X-ray crystallography. The thermodynamics of association of these mutant S peptides with S protein was measured in the presence of different concentrations of methanol and ethanol. The reduction in the strength of the hydrophobic driving force in the presence of these organic solvents was estimated from surface-tension data as well as from the dependence of the DeltaC(p) of protein/peptide binding on the alcohol concentration. The data indicated a decrease in the strength of the hydrophobic driving force of about 30-40% over a 0-30% range of the alcohol concentration. We observe that large to small substitutions destabilize the protein. However, the amount of destabilization, relative to the wild type, is independent of the alcohol concentration over the range of alcohol concentrations studied. The data clearly indicate that decreased stability of the mutants is primarily due to the loss of packing interactions rather than a reduced hydrophobic driving force and suggest a value of the hydrophobic driving force of less than 18 cal mol(-)(1) A(2). PubMed: 15823052DOI: 10.1021/bi050001+ 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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