› 3hjh

X-ray diffraction
1.95Å resolution

A rigid N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor

Released:
DOI: 10.2210/pdb3hjh/pdb
PDB entry 3hjh coloured by chain, front view.
PDB entry 3hjh coloured by chain, side view.
PDB entry 3hjh coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd.
Murphy MN, Gong P, Ralto K, Manelyte L, Savery NJ, Theis K
Nucleic Acids Res 37 6042-53 (2009)
PMID: 19700770

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151850 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription-repair-coupling factor Chain: A
Molecule details ›
Chain: A
Length: 483 amino acids
Theoretical weight: 55.09 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P30958 (Residues: 1-470; Coverage: 41%)
Gene names: JW1100, b1114, mfd
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CO 1 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P21212
Unit cell:
a: 84.062Å b: 157.65Å c: 35.964Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.21 0.257
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Prokaryotic nucleotide excision repair.
Kisker et al. (2013)
8 more

2 mentions without citation

An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd.
Murphy et al. (2009)
1 more