› 4auw

X-ray diffraction
2.9Å resolution

CRYSTAL STRUCTURE OF THE BZIP HOMODIMERIC MAFB IN COMPLEX WITH THE C- MARE BINDING SITE

Released:
DOI: 10.2210/pdb4auw/pdb
PDB entry 4auw coloured by chain, front view.
PDB entry 4auw coloured by chain, side view.
PDB entry 4auw coloured by chain, top view.
Source organisms:
Primary publication:
Expression, purification, crystallization and preliminary crystallographic analysis of the mouse transcription factor MafB in complex with its DNA-recognition motif Cmare.
Textor LC, Wilmanns M, Holton SJ
Acta Crystallogr Sect F Struct Biol Cryst Commun 63 657-61 (2007)
PMID: 17671361

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-117223 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Transcription factor MafB Chains: A, B, E, F
Molecule details ›
Chains: A, B, E, F
Length: 96 amino acids
Theoretical weight: 11.54 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P54841 (Residues: 211-305; Coverage: 29%)
Gene names: Krml, Maf1, Mafb
Sequence domains: bZIP Maf transcription factor
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
C-MARE BINDING SITE (5'-D(*AP*TP*AP*AP*TP*GP*CP*TP* GP*AP*CP*GP*TP*CP*AP*GP*CP*AP*AP*TP*T)-3') Chains: C, H
Molecule details ›
Chains: C, H
Length: 21 nucleotides
Theoretical weight: 6.44 KDa
Source organism: synthetic construct
Expression system: Not provided
C-MARE BINDING SITE (5'-D(*AP*TP*AP*AP*TP*GP*CP*TP* GP*AP*CP*GP*TP*CP*AP*GP*CP*AP*AP*TP*T)-3') Chains: D, G
Molecule details ›
Chains: D, G
Length: 21 nucleotides
Theoretical weight: 6.45 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand HG 4 x HG
Ligand DTU 1 x DTU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P43212
Unit cell:
a: 94.964Å b: 94.964Å c: 200.111Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 0.255 0.29
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 citation in other articles

Multicentric carpotarsal osteolysis is caused by mutations clustering in the amino-terminal transcriptional activation domain of MAFB.
Zankl et al. (2012)
3 more

2 mentions without citation

Gene regulation by PAX6: structural-functional correlations of missense mutants and transcriptional control of Trpm3/miR-204.
Xie et al. (2014)
1 more