Brand  (β version)

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Ligands
Code Name Style Show Link
DOB 2,4-dihydroxybenzoic acid
FAD Flavin-adenine dinucleotide
Non-standard Residues
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Glycosylation
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Modification
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Code : 1PBB   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING
Release Data : 1994-09-30
Compound :
mol_id molecule chains
1 P-HYDROXYBENZOATE HYDROXYLASE A
ec: 1.14.13.2
Source :
mol_id organism_scientific
1 Pseudomonas fluorescens  (taxid:294)
Authors : Schreuder, H.A., Mattevi, A., Hol, W.G.J.
Keywords : OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.50 Å )
Citation :

Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring

Schreuder, H.A.,Mattevi, A.,Obmolova, G.  et al.
(1994)  Biochemistry  33 : 10161 - 10170

PubMed: 7520279
DOI: 10.1021/bi00199a044

Crystal Structure of the Reduced Form of P-Hydroxybenzoate Hydroxylase Refined at 2.3 Angstroms Resolution

Schreuder, H.A.,Van Der Laan, J.M.,Swarte, M.B.A.  et al.
(1992)  Proteins  14 : 178

The Influence of Purification and Protein Heterogeneity on the Crystallization of P-Hydroxybenzoate Hydroxylase

Van Der Laan, J.M.,Swarte, M.B.A.,Groendijk, H.  et al.
(1989)  Eur.J.Biochem.  179 : 715

The Coenzyme Analogue Adenosine 5-Diphosphoribose Displaces Fad in the Active Site of P-Hydroxybenzoate Hydroxylase. An X-Ray Crystallographic Investigation

Van Der Laan, J.M.,Schreuder, H.A.,Swarte, M.B.A.  et al.
(1989)  Biochemistry  28 : 7199

Analysis of the Active Site of the Flavoprotein P-Hydroxybenzoate Hydroxylase and Some Ideas with Respect to its Reaction Mechanism

Schreuder, H.A.,Hol, W.G.J.,Drenth, J.
(1989)  Biochemistry  29 : 3101

Crystal Structure of the P-Hydroxybenzoate Hydroxylase-Substrate Complex Refined at 1.9 Angstroms Resolution. Analysis of the Enzyme-Substrate and Enzyme-Product Complexes

Schreuder, H.A.,Prick, P.A.J.,Wierenga, R.K.  et al.
(1989)  J.Mol.Biol.  208 : 679

Molecular Modeling Reveals the Possible Importance of a Carbonyl Oxygen Binding Pocket for the Catalytic Mechanism of P-Hydroxybenzoate Hydroxylase

Schreuder, H.A.,Hol, W.G.J.,Drenth, J.
(1988)  J.Biol.Chem.  263 : 3131

Crystal Structure of P-Hydroxybenzoate Hydroxylase Complexed with its Reaction Product 3,4-Dihydroxybenzoate

Schreuder, H.A.,Van Der Laan, J.M.,Hol, W.G.J.  et al.
(1988)  J.Mol.Biol.  199 : 637

Comparison of the Three-Dimensional Protein and Nucleotide Structure of the Fad-Binding Domain of P-Hydroxybenzoate Hydroxylase with the Fad-as Well as Nadph-Binding Domains of Glutathione Reductase

Wierenga, R.K.,Drenth, J.,Schulz, G.E.
(1983)  J.Mol.Biol.  167 : 725

Crystal Structure of P-Hydroxybenzoate Hydroxylase

Wierenga, R.K.,De Jong, R.J.,Kalk, K.H.  et al.
(1979)  J.Mol.Biol.  131 : 55

Crystallization and Preliminary X-Ray Investigation of P-Hydroxybenzoate Hydroxylase from Pseudomonas Fluorescens

Drenth, J.,Hol, W.G.J.,Wierenga, R.K.
(1975)  J.Biol.Chem.  250 : 5268

Chain : A
UniProt : P00438 (PHHY_PSEFL)
Reaction: EC: Evidence:
Physiological Direction:
4-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate + H2O + NADP(+) 1.14.13.2 PubMed:10025942, PubMed:10493859, PubMed:1459126, PubMed:7628466, PubMed:7756982, PubMed:9578477, PubMed:9694855
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