› 1fyl

X-ray diffraction
2.1Å resolution

SERENDIPITOUS CRYSTAL STRUCTURE CONTAINING THE HEAT SHOCK TRANSCRIPTION FACTOR'S DNA BINDING DOMAIN AND COGNATE DNA IN A HEAD-TO-HEAD ORIENTATION

Released:
DOI: 10.2210/pdb1fyl/pdb
PDB entry 1fyl coloured by chain, front view.
PDB entry 1fyl coloured by chain, side view.
PDB entry 1fyl coloured by chain, top view.
Source organism: Kluyveromyces lactis
Primary publication:
Crystal packing interaction that blocks crystallization of a site-specific DNA binding protein-DNA complex.
Littlefield O, Nelson HC
Proteins 45 219-28 (2001)
PMID: 11599025

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-218900 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Heat shock transcription factor Chains: A, B
Molecule details ›
Chains: A, B
Length: 92 amino acids
Theoretical weight: 11.09 KDa
Source organism: Kluyveromyces lactis
Expression system: Escherichia coli
UniProt:
  • Canonical: P22121 (Residues: 193-284; Coverage: 14%)
Gene names: HSF, KLLA0D03322g
Sequence domains: HSF-type DNA-binding
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
HEAD-TO-HEAD HSE Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 nucleotides
Theoretical weight: 3.73 KDa
Source organism: Kluyveromyces lactis
Expression system: Not provided

Ligands and Environments

No bound ligands
2 modified residues:
Ligand BRU 2 x BRU
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 105.14Å b: 33.73Å c: 77.84Å
α: 90° β: 118.35° γ: 90°
R-values:
R R work R free
0.213 0.213 0.3
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 citation in other articles

De novo appearance and "strain" formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor.
Park et al. (2006)
1 more

1 mention without citation

Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development.
Tschowri et al. (2014)