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.
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