1e9i | pdb_00001e9i
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ENOLASE FROM E.COLI
Overview
The crystal structure of Escherichia coli enolase (EC 4.2.1.11, phosphopyruvate hydratase), which is a component of the RNA degradosome, has been determined at 2.5 A. There are four molecules in the asymmetric, unit of the C2 cell, and in one of the molecules, flexible loops close, onto the active site. This closure mimics the conformation of the, substrate-bound intermediate. A comparison of the structure of the E. coli, enolase with the eukaryotic enolase structures available (lobster and, yeast) indicates a high degree of conservation of the hydrophobic core and, the subunit interface of this homodimeric enzyme. The dimer interface is, enriched in charged residues compared with other protein homodimers, which, may explain our observations from analytical ultracentrifugation that, dimerisation is affected by ionic strength. The putative role of enolase, in the RNA degradosome is discussed; although it was not possible to, ascribe a specific role to it, a structural role is possible.
About this Structure
1E9I is a Single protein structure of sequence from Escherichia coli with MG and SO4 as ligands. Active as Phosphopyruvate hydratase, with EC number 4.2.1.11 Full crystallographic information is available from OCA.
Reference
Crystal structure of the Escherichia coli RNA degradosome component enolase., Kuhnel K, Luisi BF, J Mol Biol. 2001 Oct 26;313(3):583-92. PMID:11676541
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