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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

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
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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