› 2jbs

X-ray diffraction
2.8Å resolution

Structure of the monooxygenase component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii

Released:
DOI: 10.2210/pdb2jbs/pdb
PDB entry 2jbs coloured by chain, front view.
PDB entry 2jbs coloured by chain, side view.
PDB entry 2jbs coloured by chain, top view.
Source organism: Acinetobacter baumannii
Primary publication:
Structure of the monooxygenase component of a two-component flavoprotein monooxygenase.
Alfieri A, Fersini F, Ruangchan N, Prongjit M, Chaiyen P, Mattevi A
Proc Natl Acad Sci U S A 104 1177-82 (2007)
PMID: 17227849

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180237 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p-hydroxyphenylacetate 3-hydroxylase, oxygenase component Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 422 amino acids
Theoretical weight: 47 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6Q272 (Residues: 1-422; Coverage: 100%)
Gene name: C2-hpah
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FMN 4 x FMN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: I222
Unit cell:
a: 94.316Å b: 183.425Å c: 284.368Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.251 0.287
Expression system: Escherichia coli BL21

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Citations

6 review citations

Flavoenzymes catalyzing oxidative aromatic ring-cleavage reactions.
Chaiyen P. (2010)
5 more

7 mentions without citation

Terpene synthases in disguise: enzymology, structure, and opportunities of non-canonical terpene synthases.
Rudolf et al. (2020)
6 more