› 1vpw

X-ray diffraction
2.7Å resolution

STRUCTURE OF THE PURR MUTANT, L54M, BOUND TO HYPOXANTHINE AND PURF OPERATOR DNA

Released:
DOI: 10.2210/pdb1vpw/pdb
PDB entry 1vpw coloured by chain, front view.
PDB entry 1vpw coloured by chain, side view.
PDB entry 1vpw coloured by chain, top view.
Source organisms:
Primary publication:
The structure of PurR mutant L54M shows an alternative route to DNA kinking.
Arvidson DN, Lu F, Faber C, Zalkin H, Brennan RG
Nat Struct Biol 5 436-41 (1998)
PMID: 9628480

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-114725 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
HTH-type transcriptional repressor PurR Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 38.11 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ACP7 (Residues: 2-341; Coverage: 100%)
Gene names: JW1650, b1658, purR
Sequence domains:
Structure domains:
DNA (5'-D(*TP*AP*CP*GP*CP*AP*AP*AP*CP*GP*TP*TP*TP*GP*CP*GP*T )-3') Chain: B
Molecule details ›
Chain: B
Length: 17 nucleotides
Theoretical weight: 5.2 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 175.89Å b: 94.93Å c: 81.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

16 citation in other articles

Geometric analysis and comparison of protein-DNA interfaces: why is there no simple code for recognition?
Pabo et al. (2000)
15 more

1 mention without citation

Novel sequence-based method for identifying transcription factor binding sites in prokaryotic genomes.
Sahota et al. (2010)