6G63

RNase E in complex with sRNA RrpA

Summary for 6G63

• Entry DOI: 10.2210/pdb6g63/pdb
• Related: 5F6C
• Descriptor: Ribonuclease E, RNA (5'-R(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*UP*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3'), ZINC ION, ... (4 entities in total)
• Functional Keywords: rnase e, small regulatory rna, rna binding protein
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 5
• Total formula weight: 238494.57

Authors

Bandyra, K.B.,Luisi, B.F. (deposition date: 2018-03-31, release date: 2018-10-03, Last modification date: 2024-05-08)

Primary citation

Bandyra, K.J.,Wandzik, J.M.,Luisi, B.F.
Substrate Recognition and Autoinhibition in the Central Ribonuclease RNase E.
Mol. Cell, 72:275-285.e4, 2018

PubMed Abstract: The endoribonuclease RNase E is a principal factor in RNA turnover and processing that helps to exercise fine control of gene expression in bacteria. While its catalytic activity can be strongly influenced by the chemical identity of the 5' end of RNA substrates, the enzyme can also cleave numerous substrates irrespective of the chemistry of their 5' ends through a mechanism that has remained largely unexplained. We report structural and functional data illuminating details of both operational modes. Our crystal structure of RNase E in complex with the sRNA RprA reveals a duplex recognition site that saddles an inter-protomer surface to help present substrates for cleavage. Our data also reveal an autoinhibitory pocket that modulates the overall activity of the ribonuclease. Taking these findings together, we propose how RNase E uses versatile modes of RNA recognition to achieve optimal activity and specificity.

PubMed: 30270108
DOI: 10.1016/j.molcel.2018.08.039

Experimental method

X-RAY DIFFRACTION (3.95 Å)