2fym
Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.
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OverviewOverview
In Escherichia coli, the glycolytic enzyme enolase is a component of the, RNA degradosome, which is an RNase E mediated assembly involved in RNA, processing and transcript turnover. The recruitment of enolase by the RNA, degradosome has been implicated in the turnover of certain transcripts, and it is mediated by a small segment of roughly a dozen residues that lie, within a natively unstructured sub-domain of RNase E. Here, we present the, crystal structure of enolase in complex with its recognition site from, RNase E at 1.6A resolution. A single molecule of the RNase E peptide binds, asymmetrically in a conserved cleft at the interface of the enolase dimer., The recognition site is well conserved in RNase E homologues in a, subfamily of the gamma-proteobacteria, including enzymes from pathogens, such as Yersinia pestis, Vibrio cholera and Salmonella sp. We suggest that, enolase is recruited into putative RNA degradosome machinery in these, bacilli, where it plays common regulatory functions.
About this StructureAbout this Structure
2FYM is a Protein complex structure of sequences from Escherichia coli with MG as ligand. Active as Phosphopyruvate hydratase, with EC number 4.2.1.11 Full crystallographic information is available from OCA.
ReferenceReference
Recognition of enolase in the Escherichia coli RNA degradosome., Chandran V, Luisi BF, J Mol Biol. 2006 Apr 21;358(1):8-15. Epub 2006 Feb 21. PMID:16516921
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