› 3fld

X-ray diffraction
2.4Å resolution

Crystal structure of the trai c-terminal domain

Released:
DOI: 10.2210/pdb3fld/pdb
PDB entry 3fld coloured by chain, front view.
PDB entry 3fld coloured by chain, side view.
PDB entry 3fld coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer.
Guogas LM, Kennedy SA, Lee JH, Redinbo MR
J Mol Biol 386 554-68 (2009)
PMID: 19136009

Function and Biology Details

Reactions catalysed: 
ATP + H(2)O = ADP + phosphate
ATP-independent breakage of single-stranded DNA, followed by passage and rejoining
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146967 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multifunctional conjugation protein TraI Chains: A, B
Molecule details ›
Chains: A, B
Length: 153 amino acids
Theoretical weight: 16.19 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P14565 (Residues: 1476-1628; Coverage: 9%)
Gene names: ECOK12F104, traI
Sequence domains: DNA helicase TraI, C-terminal
Structure domains: Helix Hairpins

Ligands and Environments

1 bound ligand:
Ligand SO4 10 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2221
Unit cell:
a: 40.8Å b: 139.751Å c: 126.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.263
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Towards an integrated model of bacterial conjugation.
Cabezón et al. (2015)
3 more

6 mentions without citation

Protein Dynamics in F-like Bacterial Conjugation.
Bragagnolo et al. (2020)
5 more