title: Molecular recognition between Escherichia coli enolase and ribonuclease E.
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.
authors.affiliation: Department of Biochemistry, University of Cambridge, England.
authors.forename: Salima
authors.initials: S
authors.lastname: Nurmohamed
authors.forename: Adam R
authors.initials: AR
authors.lastname: McKay
authors.forename: Carol V
authors.initials: CV
authors.lastname: Robinson
authors.forename: Ben F
authors.initials: BF
authors.lastname: Luisi
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010751:Phosphopyruvate Hydratase / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D016415:Sequence Alignment
chemical_list: D004722:Endoribonucleases; C022537:ribonuclease E; D010751:Phosphopyruvate Hydratase
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