1RN1

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

Summary for 1RN1

• Entry DOI: 10.2210/pdb1rn1/pdb
• Descriptor: RIBONUCLEASE T1 ISOZYME, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase(endoribonuclease)
• Biological source: Aspergillus oryzae
• Total number of polymer chains: 3
• Total formula weight: 33569.12

Authors

Arni, R.K.,Pal, G.P.,Ravichandran, K.G.,Tulinsky, A.,Walz Junior, F.G.,Metcalf, P. (deposition date: 1991-11-22, release date: 1994-01-31, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.84 Å)