2FYM
Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.
Summary for 2FYM
| Entry DOI | 10.2210/pdb2fym/pdb |
| Related | 1E9I |
| Descriptor | Enolase, Ribonuclease E, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | rna degradosome, enolase, rnase e, lyase |
| Biological source | Escherichia coli More |
| Cellular location | Cytoplasm, cytoskeleton: P0A6P9 Cytoplasm : P21513 |
| Total number of polymer chains | 6 |
| Total formula weight | 186502.50 |
| Authors | Chandran, V.,Luisi, B.F. (deposition date: 2006-02-08, release date: 2006-02-28, Last modification date: 2023-08-30) |
| Primary citation | Chandran, V.,Luisi, B.F. Recognition of Enolase in the Escherichia coli RNA Degradosome J.Mol.Biol., 358:8-15, 2006 Cited by PubMed Abstract: 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. PubMed: 16516921DOI: 10.1016/j.jmb.2006.02.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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