1nbs
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Crystal structure of the specificity domain of Ribonuclease P RNA
OverviewOverview
RNase P is the only endonuclease responsible for processing the 5' end of, transfer RNA by cleaving a precursor and leading to tRNA maturation. It, contains an RNA component and a protein component and has been identified, in all organisms. It was one of the first catalytic RNAs identified and, the first that acts as a multiple-turnover enzyme in vivo. RNase P and the, ribosome are so far the only two ribozymes known to be conserved in all, kingdoms of life. The RNA component of bacterial RNase P can catalyse, pre-tRNA cleavage in the absence of the RNase P protein in vitro and, consists of two domains: a specificity domain and a catalytic domain. Here, we report a 3.15-A resolution crystal structure of the 154-nucleotide, specificity domain of Bacillus subtilis RNase P. The structure reveals the, architecture of this domain, the interactions that maintain the overall, fold of the molecule, a large non-helical but well-structured module that, is conserved in all RNase P RNA, and the regions that are involved in, interactions with the substrate.
About this StructureAbout this Structure
1NBS is a Single protein structure of sequence from Bacillus subtilis with MG and PB as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the specificity domain of ribonuclease P., Krasilnikov AS, Yang X, Pan T, Mondragon A, Nature. 2003 Feb 13;421(6924):760-4. PMID:12610630
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