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Structure of phosphate-free ribonuclease A refined at 1.26 A.

Authors
  • Wlodawer, A
  • Svensson, L A
  • Sjölin, L
  • Gilliland, G L
Type
Published Article
Journal
Biochemistry
Publication Date
Apr 19, 1988
Volume
27
Issue
8
Pages
2705–2717
Identifiers
PMID: 3401445
Source
Medline
License
Unknown

Abstract

The structure of phosphate-free bovine ribonuclease A has been refined at 1.26-A resolution by a restrained least-squares procedure to a final R factor of 0.15. X-ray diffraction data were collected with an electronic position-sensitive detector. The final model consists of all atoms in the polypeptide chain including hydrogens, 188 water sites with full or partial occupancy, and a single molecule of 2-methyl-2-propanol. Thirteen side chains were modeled with two alternate conformations. Major changes to the active site include the addition of two waters in the phosphate-binding pocket, disordering of Gln-11, and tilting of the imidazole ring of His-119. The structure of the protein and of the associated solvent was extensively compared with three other high-resolution, refined structures of this enzyme.

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