1SRN

THE REFINED CRYSTAL STRUCTURE OF A FULLY ACTIVE SEMISYNTHETIC RIBONUCLEASE AT 1.8 ANGSTROMS RESOLUTION

Summary for 1SRN

• Entry DOI: 10.2210/pdb1srn/pdb
• Descriptor: RIBONUCLEASE A, SULFATE ION, ... (4 entities in total)
• Functional Keywords: hydrolase (nucleic acid, rna)
• Biological source: Bos taurus (cattle); More
• Cellular location: Secreted: P61823 P61823
• Total number of polymer chains: 2
• Total formula weight: 14678.34

Authors

Martin, P.D.,Doscher, M.S.,Edwards, B.F.P. (deposition date: 1990-10-05, release date: 1990-10-15, Last modification date: 2024-10-09)

Primary citation

Martin, P.D.,Doscher, M.S.,Edwards, B.F.
The refined crystal structure of a fully active semisynthetic ribonuclease at 1.8-A resolution.
J.Biol.Chem., 262:15930-15938, 1987

PubMed Abstract: A fully active, semisynthetic analog of bovine ribonuclease A, comprised of residues 1-118 of the molecule in a noncovalent complex with the synthetic peptide analog of residues 111-124, has been crystallized in space group P3(2)21 from a solution of 1.3 M ammonium sulfate and 3.0 M cesium chloride at pH 5.2. The crystallographic structure was determined by rotation and translation searches utilizing the coordinates for ribonuclease A reported by Wlodawer and Sjolin (Wlodawer, A., and Sjolin, L. (1983) Biochemistry 22, 2720-2728) and has been refined at 1.8-A resolution to an agreement factor of 0.204. Most of the structure of the semisynthetic enzyme closely resembles that found in ribonuclease A with the synthetic peptide replacing the C-terminal elements of the naturally occurring enzyme. No redundant structure is seen; residues 114-118 of the larger chain and residues 111-113 of the peptide do not appear in our map. The positions of those residues at or near the active site are very similar to, if not identical with, those previously reported by others, except for histidine 119, which occupies predominantly the B position seen as a minor site by Borkakoti et al. (Borkakoti, N., Moss, D. S., and Palmer, R. A. (1982) Acta Crystallogr. Sect. B Struct. Crystallogr. Cryst. Chem. 38,2210-2217) and not at all by Wlodawer and Sjolin (1983).

PubMed: 3680234

Experimental method

X-RAY DIFFRACTION (1.8 Å)