Ontology highlight
ABSTRACT:
SUBMITTER: Pei XY
PROVIDER: S-EPMC4652760 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Pei Xue-Yuan XY Bralley Patricia P Jones George H GH Luisi Ben F BF
Nucleic acids research 20150807 16
In diverse bacterial species, the turnover and processing of many RNAs is mediated by the ribonuclease RNase J, a member of the widely occurring metallo-β-lactamase enzyme family. We present crystal structures of Streptomyces coelicolor RNase J with bound RNA in pre- and post-cleavage states, at 2.27 Å and 2.80 Å resolution, respectively. These structures reveal snapshots of the enzyme cleaving substrate directionally and sequentially from the 5' terminus. In the pre-cleavage state, a water mole ...[more]