Molecular recognition between Escherichia coli enolase and ribonuclease E.
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.
Nurmohamed
Salima
S
Department of Biochemistry, University of Cambridge, England.
McKay
Adam R
AR
Robinson
Carol V
CV
Luisi
Ben F
BF
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
D004722:Endoribonucleases; C022537:ribonuclease E; D010751:Phosphopyruvate Hydratase
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