1RN1

THREE-DIMENSIONAL STRUCTURE OF GLN 25-RIBONUCLEASE T1 AT 1.84 ANGSTROMS RESOLUTION: STRUCTURAL VARIATIONS AT THE BASE RECOGNITION AND CATALYTIC SITES

1RN1 の概要

• エントリーDOI: 10.2210/pdb1rn1/pdb
• 分子名称: RIBONUCLEASE T1 ISOZYME, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase(endoribonuclease)
• 由来する生物種: Aspergillus oryzae
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 33569.12

構造登録者

Arni, R.K.,Pal, G.P.,Ravichandran, K.G.,Tulinsky, A.,Walz Junior, F.G.,Metcalf, P. (登録日: 1991-11-22, 公開日: 1994-01-31, 最終更新日: 2024-10-23)

主引用文献

Arni, R.K.,Pal, G.P.,Ravichandran, K.G.,Tulinsky, A.,Walz Jr., F.G.,Metcalf, P.
Three-dimensional structure of Gln25-ribonuclease T1 at 1.84-A resolution: structural variations at the base recognition and catalytic sites.
Biochemistry, 31:3126-3135, 1992

PubMed Abstract: The structure of the Gln25 variant of ribonuclease T1 (RNase T1) crystallized at pH 7 and at high ionic strength has been solved by molecular replacement using the coordinates of the Lys25-RNase T1/2'-guanylic acid (2'GMP) complex at pH 5 [Arni et al. (1988) J. Biol. Chem. 263, 15358-15368] and refined by energy minimization and stereochemically restrained least-squares minimization to a crystallographic R-factor of 14.4% at 1.84-A resolution. The asymmetric unit contains three molecules, and the final model consists of 2302 protein atoms, 3 sulfates (at the catalytic sites), and 179 solvent water molecules. The estimated root mean square (rms) error in the coordinates is 0.15 A, and the rms deviation from ideality is 0.018 A for bond lengths and 1.8 degrees for bond angles. Significant differences are observed between the three molecules in the asymmetric unit at the base recognition and catalytic sites.

PubMed: 1554699
DOI: 10.1021/bi00127a013

実験手法

X-RAY DIFFRACTION (1.84 Å)