3ZQ4

Unusual, dual endo- and exo-nuclease activity in the degradosome explained by crystal structure analysis of RNase J1

Summary for 3ZQ4

• Entry DOI: 10.2210/pdb3zq4/pdb
• Descriptor: RIBONUCLEASE J 1, ZINC ION, CALCIUM ION (3 entities in total)
• Functional Keywords: hydrolase, rna maturation
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 4
• Total formula weight: 247053.55

Authors

Newman, J.A.,Hewitt, L.,Rodrigues, C.,Solovyova, A.,Harwood, C.R.,Lewis, R.J. (deposition date: 2011-06-07, release date: 2011-09-14, Last modification date: 2023-12-20)

Primary citation

Newman, J.A.,Hewitt, L.,Rodrigues, C.,Solovyova, A.,Harwood, C.R.,Lewis, R.J.
Unusual, Dual Endo- and Exonuclease Activity in the Degradosome Explained by Crystal Structure Analysis of Rnase J1.
Structure, 19:1241-, 2011

PubMed Abstract: 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 Å resolution, analysis of which reveals it to be in an open conformation suitable for binding substrate RNA. RNase J is a member of the β-CASP family of zinc-dependent metallo-β-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.

PubMed: 21893285
DOI: 10.1016/J.STR.2011.06.017

Experimental method

X-RAY DIFFRACTION (3 Å)