ARN

@article{,

title = {RNase P: At last, the key finds its lock.},

author = {B Masquida and E Westhof},

url = {http://www.ncbi.nlm.nih.gov/pubmed/21803972},

doi = {10.1261/rna.2841511},

isbn = {21803972},

year  = {2011},

date = {2011-01-01},

journal = {RNA},

volume = {17},

number = {9},

pages = {1615-1618},

abstract = {Apart from the ribosome, the crystal structure of the bacterial RNase P in complex with a tRNA, reported by Reiter and colleagues recently, constitutes the first example of a multiple turnover RNA enzyme. Except in rare exceptions, RNase P is ubiquitous and, like the ribosome, is older than the initial branch point of the phylogenetic tree. Importantly, the structure shows how the RNA and the protein moieties cooperate to process the pre-tRNA substrates. The catalytic site comprises some critical RNA residues spread over the secondary structure but gathered in a compact volume next to the protein, which helps recognize and orient the substrate. The discussion here outlines some important aspects of that crystal structure, some of which could apply to RNA molecules in general.},

keywords = {RNase P Multiple-turnover ribozyme RNA–RNA interactions Molecular evolution Crystallography, Unité ARN, WESTHOF},

pubstate = {published},

tppubtype = {article}

}