2VMK

Crystal Structure of E. coli RNase E Apoprotein - Catalytic Domain

Summary for 2VMK

• Entry DOI: 10.2210/pdb2vmk/pdb
• Related: 1SLJ 1SMX 1SN8 2BX2 2C0B 2C4R 2FYM 2VRT
• Descriptor: RIBONUCLEASE E, SULFATE ION, ZINC ION (3 entities in total)
• Functional Keywords: nuclease, hydrolase, cytoplasm, rna-binding, rna turnover, endonuclease, rna processing
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm: P21513
• Total number of polymer chains: 4
• Total formula weight: 232054.16

Authors

Koslover, D.J.,Callaghan, A.J.,Marcaida, M.J.,Martick, M.,Scott, W.G.,Luisi, B.F. (deposition date: 2008-01-28, release date: 2008-07-22, Last modification date: 2023-12-13)

Primary citation

Koslover, D.J.,Callaghan, A.J.,Marcaida, M.J.,Garman, E.F.,Martick, M.,Scott, W.G.,Luisi, B.F.
The Crystal Structure of the Escherichia Coli Rnase E Apoprotein and a Mechanism for RNA Degradation.
Structure, 16:1238-, 2008

PubMed Abstract: 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.

PubMed: 18682225
DOI: 10.1016/J.STR.2008.04.017

Experimental method

X-RAY DIFFRACTION (3.3 Å)