In:
Acta Crystallographica Section D Biological Crystallography, International Union of Crystallography (IUCr), Vol. 66, No. 9 ( 2010-09-01), p. 1036-1040
Abstract:
In Escherichia coli and many other bacterial species, the glycolytic enzyme enolase is a component of the multi-enzyme RNA degradosome, an assembly that is involved in RNA processing and degradation. Enolase is recruited into the degradosome through interactions with a small recognition motif located within the degradosome-scaffolding domain of RNase E. Here, the crystal structure of enolase bound to its cognate site from RNase E (residues 823–850) at 1.9 Å resolution is presented. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E.
Type of Medium:
Online Resource
ISSN:
0907-4449
DOI:
10.1107/S0907444910030015
DOI:
10.1107/S0907444910030015/hv5161sup1.pdf
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2010
detail.hit.zdb_id:
2968623-4
SSG:
12
SSG:
13
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