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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.

Original publication




Journal article


Acta Crystallogr D Biol Crystallogr

Publication Date





1036 - 1040


Amino Acid Sequence, Crystallography, X-Ray, Endoribonucleases, Escherichia coli, Models, Molecular, Molecular Sequence Data, Phosphopyruvate Hydratase, Protein Binding, Protein Interaction Domains and Motifs, Protein Structure, Quaternary, Sequence Alignment