› 1ega

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF A WIDELY CONSERVED GTPASE ERA

Released:
DOI: 10.2210/pdb1ega/pdb
PDB entry 1ega coloured by chain, front view.
PDB entry 1ega coloured by chain, side view.
PDB entry 1ega coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif.
Chen X, Court DL, Ji X
Proc Natl Acad Sci U S A 96 8396-401 (1999)
PMID: 10411886

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139100 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase Era Chains: A, B
Molecule details ›
Chains: A, B
Length: 301 amino acids
Theoretical weight: 33.86 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P06616 (Residues: 1-301; Coverage: 100%)
Gene names: JW2550, b2566, era, rbaA, sdgE
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 86.79Å b: 67.56Å c: 87.29Å
α: 90° β: 115.82° γ: 90°
R-values:
R R work R free
0.243 0.243 0.298

Quick links

Citations

12 review citations

Structure-function relationships of the G domain, a canonical switch motif.
Wittinghofer et al. (2011)
11 more

15 mentions without citation

The universally conserved prokaryotic GTPases.
Verstraeten et al. (2011)
14 more