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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.
Crystal structure of a bacterial ribonuclease P RNA.,Kazantsev AV, Krivenko AA, Harrington DJ, Holbrook SR, Adams PD, Pace NR Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13392-7. Epub 2005 Sep 12. PMID:16157868[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Kazantsev AV, Krivenko AA, Harrington DJ, Holbrook SR, Adams PD, Pace NR. Crystal structure of a bacterial ribonuclease P RNA. Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13392-7. Epub 2005 Sep 12. PMID:16157868 doi:0506662102
