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

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The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. / Koslover, D.; Callaghan, Anastasia; Marcaida, M.; Garman, E.; Martick, M.; Scott, W.; Luisi, B.

In: Structure, Vol. 16, No. 8, 2008, p. 1238-1244.

Research output: Contribution to journalArticle

Harvard

Koslover, D, Callaghan, A, Marcaida, M, Garman, E, Martick, M, Scott, W & Luisi, B 2008, 'The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation', Structure, vol. 16, no. 8, pp. 1238-1244. https://doi.org/10.1016/j.str.2008.04.017

APA

Koslover, D., Callaghan, A., Marcaida, M., Garman, E., Martick, M., Scott, W., & Luisi, B. (2008). The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. Structure, 16(8), 1238-1244. https://doi.org/10.1016/j.str.2008.04.017

Vancouver

Author

Koslover, D. ; Callaghan, Anastasia ; Marcaida, M. ; Garman, E. ; Martick, M. ; Scott, W. ; Luisi, B. / The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. In: Structure. 2008 ; Vol. 16, No. 8. pp. 1238-1244.

Bibtex

@article{0967947cf43c424f8059d169e66d2faa,
title = "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 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.",
author = "D. Koslover and Anastasia Callaghan and M. Marcaida and E. Garman and M. Martick and W. Scott and B. Luisi",
year = "2008",
doi = "10.1016/j.str.2008.04.017",
language = "English",
volume = "16",
pages = "1238--1244",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "8",

}

RIS

TY - JOUR

T1 - The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation

AU - Koslover, D.

AU - Callaghan, Anastasia

AU - Marcaida, M.

AU - Garman, E.

AU - Martick, M.

AU - Scott, W.

AU - Luisi, B.

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

U2 - 10.1016/j.str.2008.04.017

DO - 10.1016/j.str.2008.04.017

M3 - Article

VL - 16

SP - 1238

EP - 1244

JO - Structure

JF - Structure

SN - 0969-2126

IS - 8

ER -

ID: 35632