Three-dimensional structure of ribonuclease Ms*3'-guanylic acid complex at 2.5 A resolution.
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.
Nonaka
T
T
Faculty of Engineering, Nagaoka University of Technology, Niigato, Japan.
Mitsui
Y
Y
Irie
M
M
Nakamura
K T
KT
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
D006157:Guanosine Monophosphate; D004722:Endoribonucleases; C022543:ribonuclease T(2)