Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Molecular recognition between Escherichia coli enolase and ribonuclease E.,Nurmohamed S, McKay AR, Robinson CV, Luisi BF Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1036-40. Epub 2010 Aug 13. PMID:20823555[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nurmohamed S, McKay AR, Robinson CV, Luisi BF. Molecular recognition between Escherichia coli enolase and ribonuclease E. Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1036-40. Epub 2010 Aug 13. PMID:20823555 doi:10.1107/S0907444910030015
