Structural highlights
Publication Abstract from PubMed
RNase J is an essential enzyme in Bacillus subtilis with unusual dual endonuclease and 5'-to-3' exonuclease activities that play an important role in the maturation and degradation of mRNA. RNase J is also a component of the recently identified "degradosome" of B. subtilis. We report the crystal structure of RNase J1 from B. subtilis to 3.0 A resolution, analysis of which reveals it to be in an open conformation suitable for binding substrate RNA. RNase J is a member of the beta-CASP family of zinc-dependent metallo-beta-lactamases. We have exploited this similarity in constructing a model for an RNase J1:RNA complex. Analysis of this model reveals candidate-stacking interactions with conserved aromatic side chains, providing a molecular basis for the observed enzyme activity. Comparisons of the B. subtilis RNase J structure with related enzymes reveal key differences that provide insights into conformational changes during catalysis and the role of the C-terminal domain.
Unusual, Dual Endo- and Exonuclease Activity in the Degradosome Explained by Crystal Structure Analysis of RNase J1.,Newman JA, Hewitt L, Rodrigues C, Solovyova A, Harwood CR, Lewis RJ Structure. 2011 Sep 7;19(9):1241-51. PMID:21893285[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Newman JA, Hewitt L, Rodrigues C, Solovyova A, Harwood CR, Lewis RJ. Unusual, Dual Endo- and Exonuclease Activity in the Degradosome Explained by Crystal Structure Analysis of RNase J1. Structure. 2011 Sep 7;19(9):1241-51. PMID:21893285 doi:10.1016/j.str.2011.06.017
