PDBe 2fym

X-ray diffraction
1.6Å resolution

Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.

Released:
Primary publication:
Recognition of enolase in the Escherichia coli RNA degradosome.
J. Mol. Biol. 358 8-15 (2006)
PMID: 16516921

Function and Biology Details

Reactions catalysed:
2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. 
Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Enolase Chains: A, C, D, F
Molecule details ›
Chains: A, C, D, F
Length: 431 amino acids
Theoretical weight: 45.58 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6P9 (Residues: 2-432; Coverage: 100%)
Gene names: JW2750, b2779, eno
Sequence domains:
Structure domains:
Ribonuclease E Chains: B, E
Molecule details ›
Chains: B, E
Length: 18 amino acids
Theoretical weight: 2.05 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided
UniProt:
  • Canonical: P21513 (Residues: 833-850; Coverage: 2%)
Gene names: JW1071, ams, b1084, hmp1, rne

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4, ESRF BEAMLINE ID29, RIGAKU
Spacegroup: P21
Unit cell:
a: 77.054Å b: 124.201Å c: 96.076Å
α: 90° β: 90.58° γ: 90°
R-values:
R R work R free
0.167 0.165 0.201
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided