title: Three-dimensional structure of ribonuclease Ms*3'-guanylic acid complex at 2.5 A resolution.
abstract: The crystal structure of ribonuclease Ms*3'-guanylic acid complex has been determined by molecular replacement methods based on the known structure of ribonuclease T1. The pattern of hydrogen-bonds between the enzyme and the guanine base is similar to that discovered by Arni et al. [( 1988) J. Biol. Chem. 263, 15358-15368] in the crystal structure of ribonuclease T1*2'-guanylic acid complex. As for the possible general base in the trans-phosphorylation step of the catalysis, 0 epsilon 1 of Glu57 is within the hydrogen-bond distance (2.7 A) of the 2'-0 of the nucleotide while N epsilon 2 of His39 is significantly more distant (3.4 A) from the 2'-0.
authors.affiliation: Faculty of Engineering, Nagaoka University of Technology, Niigato, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Nonaka
authors.forename: Y
authors.initials: Y
authors.lastname: Mitsui
authors.forename: M
authors.initials: M
authors.lastname: Irie
authors.forename: K T
authors.initials: KT
authors.lastname: Nakamura
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism; D006157:Guanosine Monophosphate / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D006157:Guanosine Monophosphate; D004722:Endoribonucleases; C022543:ribonuclease T(2)