› 1hxd

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN

Released:
DOI: 10.2210/pdb1hxd/pdb
PDB entry 1hxd coloured by chain, front view.
PDB entry 1hxd coloured by chain, side view.
PDB entry 1hxd coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
Weaver LH, Kwon K, Beckett D, Matthews BW
Proc Natl Acad Sci U S A 98 6045-50 (2001)
PMID: 11353844

Function and Biology Details

Reaction catalysed: 
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional ligase/repressor BirA Chains: A, B
Molecule details ›
Chains: A, B
Length: 321 amino acids
Theoretical weight: 35.35 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06709 (Residues: 1-321; Coverage: 100%)
Gene names: JW3941, b3973, bioR, birA, dhbB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand BTN 2 x BTN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 104.9Å b: 108.9Å c: 143.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Coupling of folding and binding for unstructured proteins.
Dyson et al. (2002)
12 more

19 mentions without citation

Engineering central metabolic pathways for high-level flavonoid production in Escherichia coli.
Leonard et al. (2007)
18 more