1E9I

Enolase from E.coli

Summary for 1E9I

• Entry DOI: 10.2210/pdb1e9i/pdb
• Related: 1EBG 1EBH 1ELS 1NEL 1ONE 1PDY 1PDZ 2ONE 3ENL 4ENL 5ENL 6ENL 7ENL
• Descriptor: ENOLASE, MAGNESIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: degradosome, lyase
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm, cytoskeleton: P08324
• Total number of polymer chains: 4
• Total formula weight: 182532.06

Authors

Kuhnel, K.,Carpousis, A.J.,Luisi, B. (deposition date: 2000-10-17, release date: 2001-03-15, Last modification date: 2023-12-13)

Primary citation

Kuhnel, K.,Luisi, B.
Crystal Structure of the Escherichia Coli RNA Degradosome Component Enolase
J.Mol.Biol., 313:583-, 2001

PubMed Abstract: 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.

PubMed: 11676541
DOI: 10.1006/JMBI.2001.5065

Experimental method

X-RAY DIFFRACTION (2.48 Å)