Molecular recognition between Escherichia coli enolase and ribonuclease E.

Nurmohamed S, McKay AR, Robinson CV, Luisi BF

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.

Keywords:

Amino Acid Sequence

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Crystallography, X-Ray

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Endoribonucleases

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Escherichia coli

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Models, Molecular

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Molecular Sequence Data

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Phosphopyruvate Hydratase

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Protein Binding

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Protein Interaction Domains and Motifs

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Protein Structure, Quaternary

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Sequence Alignment