Crystal structure of a bacterial ribonuclease P RNA.
The x-ray crystal structure of a 417-nt ribonuclease P RNA from Bacillus stearothermophilus was solved to 3.3-A resolution. This RNA enzyme is constructed from a number of coaxially stacked helical domains joined together by local and long-range interactions. These helical domains are arranged to form a remarkably flat surface, which is implicated by a wealth of biochemical data in the binding and cleavage of the precursors of transfer RNA substrate. Previous photoaffinity crosslinking data are used to position the substrate on the crystal structure and to identify the chemically active site of the ribozyme. This site is located in a highly conserved core structure formed by intricately interlaced long-range interactions between interhelical sequences.
Kazantsev
Alexei V
AV
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.
Krivenko
Angelika A
AA
Harrington
Daniel J
DJ
Holbrook
Stephen R
SR
Adams
Paul D
PD
Pace
Norman R
NR
D001426:Bacterial Proteins / Q000737:chemistry; D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D001411:Geobacillus stearothermophilus / Q000737:chemistry* / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000737:chemistry*; D016337:RNA, Catalytic / Q000737:chemistry*; D043262:Ribonuclease P / Q000737:chemistry*
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D043262:Ribonuclease P