1A5Q

P93A VARIANT OF BOVINE PANCREATIC RIBONUCLEASE A

1A5Q の概要

• エントリーDOI: 10.2210/pdb1a5q/pdb
• 分子名称: RIBONUCLEASE A, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase (nucleic acid, rna), hydrolase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted: P61823
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13778.35

構造登録者

Pearson, M.A.,Karplus, P.A.,Dodge, R.W.,Laity, J.H.,Scheraga, H.A. (登録日: 1998-02-17, 公開日: 1998-05-27, 最終更新日: 2024-10-30)

主引用文献

Pearson, M.A.,Karplus, P.A.,Dodge, R.W.,Laity, J.H.,Scheraga, H.A.
Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A.
Protein Sci., 7:1255-1258, 1998

PubMed Abstract: The Tyr92-Pro93 peptide group of bovine pancreatic ribonuclease A (RNase A) exists in the cis conformation in the native state. From unfolding/refolding kinetic studies of the disulfide-intact wild-type protein and of a variant in which Pro93 had been replaced by Ala, it had been suggested that the Tyr92-Ala93 peptide group also exists in the cis conformation in the native state. Here, we report the crystal structure of the P93A variant. Although there is disorder in the region of residues 92 and 93, the best structural model contains a cis peptide at this position, lending support to the results of the kinetics experiments. We also report the crystal structure of the C[40, 95]A variant, which is an analog of the major rate-determining three-disulfide intermediate in the oxidative folding of RNase A, missing the 40-95 disulfide bond. As had been detected by NMR spectroscopy, the crystal structure of this analog shows disorder in the region surrounding the missing disulfide. However, the global chain fold of the remainder of the protein, including the disulfide bond between Cys65 and Cys72, appears to be unaffected by the mutation.

PubMed: 9605332

実験手法

X-RAY DIFFRACTION (2.3 Å)