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The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation.

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 ...

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Publication status:
Published

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Publisher copy:
10.1016/j.str.2008.04.017

Authors


Koslover, DJ More by this author
Callaghan, AJ More by this author
Marcaida, MJ More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Martick, M More by this author
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Journal:
Structure (London, England : 1993)
Volume:
16
Issue:
8
Pages:
1238-1244
Publication date:
2008-08-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:419704df-5b57-40f6-bedf-b9443b6b0b6f
Source identifiers:
100742
Local pid:
pubs:100742

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