PMID:20823555
| Citation |
Nurmohamed, S, McKay, AR, Robinson, CV and Luisi, BF (2010) Molecular recognition between Escherichia coli enolase and ribonuclease E. Acta Crystallogr. D Biol. Crystallogr. 66:1036-40 |
|---|---|
| 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 A resolution is presented. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E. |
| Links |
PubMed PMC2935283 Online version:10.1107/S0907444910030015 |
| Keywords |
Amino Acid Sequence; Crystallography, X-Ray; Endoribonucleases/chemistry; Endoribonucleases/metabolism; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Phosphopyruvate Hydratase/chemistry; Phosphopyruvate Hydratase/metabolism; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Quaternary; Sequence Alignment |
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