› 2yyj

X-ray diffraction
1.66Å resolution

Crystal structure of the oxygenase component (HpaB) of 4-hydroxyphenylacetate 3-monooxygenase complexed with FAD and 4-hydroxyphenylacetate

Released:
DOI: 10.2210/pdb2yyj/pdb
PDB entry 2yyj coloured by chain, front view.
PDB entry 2yyj coloured by chain, side view.
PDB entry 2yyj coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8.
Kim SH, Hisano T, Takeda K, Iwasaki W, Ebihara A, Miki K
J Biol Chem 282 33107-17 (2007)
PMID: 17804419

Function and Biology Details

Reaction catalysed: 
4-hydroxyphenylacetate + FADH(2) + O(2) = 3,4-dihydroxyphenylacetate + FAD + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178032 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxyphenylacetate 3-monooxygenase oxygenase component Chain: A
Molecule details ›
Chain: A
Length: 481 amino acids
Theoretical weight: 54.37 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SJP8 (Residues: 1-481; Coverage: 100%)
Gene name: TTHA0960
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
2 bound ligands:
Ligand SO4 6 x SO4
Ligand 4HP 2 x 4HP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: I222
Unit cell:
a: 90.894Å b: 98.466Å c: 130.586Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.167
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Mechanisms of reduced flavin transfer in the two-component flavin-dependent monooxygenases.
Sucharitakul et al. (2014)
1 more

12 mentions without citation

Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities.
Heine et al. (2018)
11 more