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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.

SUBMITTER: Nurmohamed S

PROVIDER: S-EPMC2935283 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

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Molecular recognition between Escherichia coli enolase and ribonuclease E.

Nurmohamed Salima S McKay Adam R AR Robinson Carol V CV Luisi Ben F BF

Acta crystallographica. Section D, Biological crystallography 20100813 Pt 9

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 ...[more]

PMID: 20823555

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