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› 5mll

X-ray diffraction
1.9Å resolution

Structure of HpDprA at 1.9 Angstroms resolution

Released:
DOI: 10.2210/pdb5mll/pdb
Model geometry
Fit model/data
PDB entry 5mll coloured by chain, front view.
PDB entry 5mll coloured by chain, side view.
PDB entry 5mll coloured by chain, top view.
Source organism: Helicobacter pylori 26695
Primary publication:
The C-terminal domain of HpDprA is a DNA-binding winged helix domain that does not bind double-stranded DNA.
Lisboa J, Celma L, Sanchez D, Marquis M, Andreani J, Guérois R, Ochsenbein F, Durand D, Marsin S, Cuniasse P, Radicella JP, Quevillon-Cheruel S
FEBS J 286 1941-1958 (2019)
PMID: 30771270

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127712 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA processing chain A (DprA) Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 24.45 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: O25100 (Residues: 3-221; Coverage: 81%)
Gene name: HP_0333
Sequence domains: DNA recombination-mediator protein A
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 40.38Å b: 67.58Å c: 159.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.247
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Natural Transformation in Deinococcus radiodurans: A Genetic Analysis Reveals the Major Roles of DprA, DdrB, RecA, RecF, and RecO Proteins.
Ithurbide et al. (2020)