3H8A

Crystal structure of E. coli enolase bound to its cognate RNase E recognition domain

Summary for 3H8A

Entry DOI	10.2210/pdb3h8a/pdb
Descriptor	Enolase, RNase E, MAGNESIUM ION, ... (4 entities in total)
Functional Keywords	glycolytic enzyme, protein-protein interaction, lyase, metal-binding, lyase-protein binding complex, lyase/protein binding
Biological source	Escherichia coli More
Cellular location	Cytoplasm, cytoskeleton: P0A6P9
Total number of polymer chains	6
Total formula weight	188971.03
Authors	Nurmohamed, S.,Luisi, B.F. (deposition date: 2009-04-29, release date: 2010-04-14, Last modification date: 2023-09-06)
Primary citation	Nurmohamed, S.,McKay, A.R.,Robinson, C.V.,Luisi, B.F. Molecular recognition between Escherichia coli enolase and ribonuclease E. Acta Crystallogr.,Sect.D, 66:1036-1040, 2010 Cited by PubMed 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. PubMed: 20823555 DOI: 10.1107/S0907444910030015 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation