2VRT: Crystal Structure Of E. Coli Rnase E Possessing M1 Rna Fragments - Catalytic Domain

RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli. Here, we present the crystal structure of the E. coli RNase E catalytic domain in the apo-state at 3.3 A. This structure indicates that, upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site. The structural data suggest a mechanism of RNA recognition and cleavage that explains the enzyme's preference for substrates possessing a 5'-monophosphate and accounts for the protective effect of a triphosphate cap for most transcripts. Internal flexibility within the quaternary structure is also observed, a finding that has implications for recognition of structured RNA substrates and for the mechanism of internal entry for a subset of substrates that are cleaved without 5'-end requirements.
PDB ID: 2VRTDownload
MMDB ID: 65585
PDB Deposition Date: 2008/4/14
Updated in MMDB: 2012/09
Experimental Method:
x-ray diffraction
Resolution: 3.5  Å
Source Organism:
Similar Structures:
Biological Unit for 2VRT: dimeric; determined by author and by software (PQS)
Molecular Components in 2VRT
Label Count Molecule
Protein (1 molecule)
Ribonuclease E(Gene symbol: rne)
Molecule annotation
Nucleotide(1 molecule)
Molecule annotation
Chemical (1 molecule)
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Citing MMDB