Molecular recognition between Escherichia coli enolase and ribonuclease E

✍ Scribed by Nurmohamed, Salima (author);McKay, Adam R. (author);Robinson, Carol V. (author);Luisi, Ben F. (author)

• Book ID: 104478582
• Publisher: International Union of Crystallography
• Year: 2010
• Tongue: English
• Weight: 763 KB
• Volume: 66
• Category: Article
• ISSN: 0907-4449
• DOI: 10.1107/s0907444910030015

✦ Synopsis

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 Å resolution is presented. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E.