› 2wwy

X-ray diffraction
2.9Å resolution

Structure of human RECQ-like helicase in complex with a DNA substrate

Released:
DOI: 10.2210/pdb2wwy/pdb
PDB entry 2wwy coloured by chain, front view.
PDB entry 2wwy coloured by chain, side view.
PDB entry 2wwy coloured by chain, top view.
Source organisms:
Primary publication:
Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: insights from DNA complex structures.
Pike AC, Gomathinayagam S, Swuec P, Berti M, Zhang Y, Schnecke C, Marino F, von Delft F, Renault L, Costa A, Gileadi O, Vindigni A
Proc Natl Acad Sci U S A 112 4286-91 (2015)
PMID: 25831490

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-115918 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
ATP-dependent DNA helicase Q1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 591 amino acids
Theoretical weight: 67.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P46063 (Residues: 48-619; Coverage: 88%)
Gene names: RECQ1, RECQL, RECQL1
Sequence domains:
Structure domains:
DNA OLIGO (27BP) Chains: O, Q, R, T
Molecule details ›
Chains: O, Q, R, T
Length: 27 nucleotides
Theoretical weight: 8.21 KDa
Source organism: synthetic construct
Expression system: Not provided
5'-D(*DA DG DC DG DT DC DG DA DG DA DT DC DCP)-3' Chains: P, S
Molecule details ›
Chains: P, S
Length: 13 nucleotides
Theoretical weight: 3.98 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand SO4 4 x SO4
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 58.333Å b: 174.218Å c: 100.229Å
α: 90° β: 93.31° γ: 90°
R-values:
R R work R free
0.2 0.198 0.236
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

11 review citations

DNA Polymerase θ: A Unique Multifunctional End-Joining Machine.
Black et al. (2016)
10 more

23 mentions without citation

Human RecQ helicases in DNA repair, recombination, and replication.
Croteau et al. (2014)
22 more