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Crystal structure of a bacterial ribonuclease P RNA
Crystal structure of a bacterial ribonuclease P RNA.
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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 AV, Krivenko AA, Harrington DJ, Holbrook SR, Adams PD, Pace NR
Proceedings of the National Academy of Sciences of the United States of America
2005-09-20 00:00
102
38
13392-7
Bacillus stearothermophilus,Bacterial Proteins,Base Sequence,Binding Sites,Crystallography, X-Ray,Models, Molecular,Molecular Sequence Data,Nucleic Acid Conformation,RNA, Bacterial,RNA, Catalytic,Ribonuclease P,Bacterial Proteins,RNA, Bacterial,RNA, Catalytic,Ribonuclease P
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA
Proc. Natl. Acad. Sci. U.S.A.
NIGMS GM 34527
0027-8424
10.1073/pnas.0506662102
0506662102
914
True
16157868
