1nbs: Difference between revisions

Revision as of 02:20, 3 May 2008

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. 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 Page seeded by OCA on Sat May 3 02:20:35 2008

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OCA

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 '''Crystal structure of the specificity domain of Ribonuclease P RNA'''
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 [[Category: Pan, T.]]
 [[Category: Yang, X.]]
-[[Category: p rna]]
+[[Category: P rna]]
-[[Category: ribonuclease p rna]]
+[[Category: Ribonuclease p rna]]
-[[Category: s-domain]]
+[[Category: S-domain]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:20:35 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:15 2008''