› 1grj

X-ray diffraction
2.2Å resolution

GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1grj/pdb
PDB entry 1grj coloured by chain, front view.
PDB entry 1grj coloured by chain, side view.
PDB entry 1grj coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the GreA transcript cleavage factor from Escherichia coli.
Stebbins CE, Borukhov S, Orlova M, Polyakov A, Goldfarb A, Darst SA
Nature 373 636-40 (1995)
PMID: 7854424

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141435 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription elongation factor GreA Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.66 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A6W5 (Residues: 1-158; Coverage: 100%)
Gene names: JW3148, b3181, greA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 102.357Å b: 42.66Å c: 39.904Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.32
Expression system: Not provided

Quick links

Citations

15 review citations

Basic mechanisms of transcript elongation and its regulation.
Uptain et al. (1997)
14 more

19 mentions without citation

The Blueprint of a Minimal Cell: MiniBacillus.
Reuß et al. (2016)
18 more