4OXP

X-ray crystal structure of the S1 and 5'-sensor domains of RNase E from Caulobacter crescentus

Summary for 4OXP

• Entry DOI: 10.2210/pdb4oxp/pdb
• Descriptor: Ribonuclease E (2 entities in total)
• Functional Keywords: rnase e, endoribonuclease, hydrolase
• Biological source: Caulobacter crescentus
• Cellular location: Cytoplasm : Q9A749
• Total number of polymer chains: 1
• Total formula weight: 32978.07

Authors

Voss, J.E.,Luisi, B.F.L.,Hardwick, S.W. (deposition date: 2014-02-06, release date: 2014-12-03, Last modification date: 2023-12-27)

Primary citation

Voss, J.E.,Luisi, B.F.,Hardwick, S.W.
Molecular recognition of RhlB and RNase D in the Caulobacter crescentus RNA degradosome.
Nucleic Acids Res., 42:13294-13305, 2014

PubMed Abstract: The endoribonuclease RNase E is a key enzyme in RNA metabolism for many bacterial species. In Escherichia coli, RNase E contributes to the majority of RNA turnover and processing events, and the enzyme has been extensively characterized as the central component of the RNA degradosome assembly. A similar RNA degradosome assembly has been described in the α-proteobacterium Caulobacter crescentus, with the interacting partners of RNase E identified as the Kreb's cycle enzyme aconitase, a DEAD-box RNA helicase RhlB and the exoribonuclease polynucleotide phosphorylase. Here we report that an additional degradosome component is the essential exoribonuclease RNase D, and its recognition site within RNase E is identified. We show that, unlike its E. coli counterpart, C. crescentus RhlB interacts directly with a segment of the N-terminal catalytic domain of RNase E. The crystal structure of a portion of C. crescentus RNase E encompassing the helicase-binding region is reported. This structure reveals that an inserted segment in the S1 domain adopts an α-helical conformation, despite being predicted to be natively unstructured. We discuss the implications of these findings for the organization and mechanisms of the RNA degradosome.

PubMed: 25389270
DOI: 10.1093/nar/gku1134

Experimental method

X-RAY DIFFRACTION (2.1 Å)