X-ray diffraction
2.4Å resolution

Crystal Structure of BmrR Bound to DNA at 2.4A Resolution


Function and Biology Details

Reactions catalysed:
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
D-galactose + O(2) = D-galacto-hexodialdose + H(2)O(2)
Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N(6)-L-lysine
(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH
3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol hexakisphosphate
ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + cellular protein(Side 2)
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
A 2'-deoxyribonucleoside 5'-monophosphate + H(2)O = a 2'-deoxyribonucleoside + phosphate
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
NTP + H(2)O = NDP + phosphate
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
A phosphate monoester + H(2)O = an alcohol + phosphate
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
ATP-dependent cleavage of peptide bonds with broad specificity.
Diphosphate + H(2)O = 2 phosphate
L-lysine + NADPH + O(2) = N(6)-hydroxy-L-lysine + NADP(+) + H(2)O
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
ATP + H(2)O = ADP + phosphate
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
ATP + thymidine = ADP + thymidine 5'-phosphate
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA
Chorismate = prephenate
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Multidrug-efflux transporter 1 regulator Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 32.62 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
  • Canonical: P39075 (Residues: 1-278; Coverage: 100%)
Gene names: BSU24020, bmr1R, bmrR
Sequence domains:
Structure domains:
Molecule details ›
Chain: B
Length: 23 nucleotides
Theoretical weight: 7.06 KDa
Source organism: Bacillus subtilis
Expression system: Not provided

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P4322
Unit cell:
a: 107.28Å b: 107.28Å c: 145.7Å
α: 90° β: 90° γ: 90°
R R work R free
0.227 0.227 0.267
Expression systems:
  • Escherichia coli
  • Not provided