2a2e
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Crystal structure of the RNA subunit of Ribonuclease P. Bacterial A-type.
OverviewOverview
Transfer RNA (tRNA) is produced as a precursor molecule that needs to be, processed at its 3' and 5' ends. Ribonuclease P is the sole endonuclease, responsible for processing the 5' end of tRNA by cleaving the precursor, and leading to tRNA maturation. It was one of the first catalytic RNA, molecules identified and consists of a single RNA component in all, organisms and only one protein component in bacteria. It is a true, multi-turnover ribozyme and one of only two ribozymes (the other being the, ribosome) that are conserved in all kingdoms of life. Here we show the, crystal structure at 3.85 A resolution of the RNA component of Thermotoga, maritima ribonuclease P. The entire RNA catalytic component is revealed, as well as the arrangement of the two structural domains. The structure, shows the general architecture of the RNA molecule, the inter- and, intra-domain interactions, the location of the universally conserved, regions, the regions involved in pre-tRNA recognition and the location of, the active site. A model with bound tRNA is in agreement with all existing, data and suggests the general basis for RNA-RNA recognition by this, ribozyme.
About this StructureAbout this Structure
2A2E is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the RNA component of bacterial ribonuclease P., Torres-Larios A, Swinger KK, Krasilnikov AS, Pan T, Mondragon A, Nature. 2005 Sep 22;437(7058):584-7. Epub 2005 Aug 21. PMID:16113684
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