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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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H.A.Schreuder,
A.Mattevi,
G.Obmolova,
K.H.Kalk,
W.G.Hol,
F.J.Van der bolt,
W.J.Van berkel.
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Ref.
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Biochemistry, 1994,
33,
10161-10170.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Abstract
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The crystal structures of wild-type p-hydroxybenzoate hydroxylase from
Pseudomonas fluorescens, complexed with the substrate analogues 4-aminobenzoate,
2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate have been determined at
2.3-, 2.5-, and 2.8-A resolution, respectively. In addition, the crystal
structure of a Tyr222Ala mutant, complexed with 2-hydroxy-4-aminobenzoate, has
been determined at 2.7-A resolution. The structures have been refined to R
factors between 14.5% and 15.8% for data between 8.0 A and the high-resolution
limit. The differences between these complexes and the wild-type
enzyme-substrate complex are all concentrated in the active site region. Binding
of substrate analogues bearing a 4-amino group (4-aminobenzoate and
2-hydroxy-4-aminobenzoate) leads to binding of a water molecule next to the
active site Tyr385. As a result, a continuous hydrogen-bonding network is
present between the 4-amino group of the substrate analogue and the side chain
of His72. It is likely that this hydrogen-bonding network is transiently present
during normal catalysis, where it may or may not function as a proton channel
assisting the deprotonation of the 4-hydroxyl group of the normal substrate upon
binding to the active site. Binding of substrate analogues bearing a hydroxyl
group at the 2-position (2,4-dihydroxybenzoate and 2-hydroxy-4-aminobenzoate)
leads to displacement of the flavin ring from the active site. The flavin is no
longer in the active site (the "in" conformation) but is in the cleft leading to
the active site instead (the "out" conformation). It is proposed that movement
of the FAD out of the active site may provide an entrance for the substrate to
enter the active site and an exit for the product to leave.
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Secondary reference #1
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Title
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Crystal structure of the reduced form of p-Hydroxybenzoate hydroxylase refined at 2.3 a resolution.
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Authors
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H.A.Schreuder,
J.M.Van der laan,
M.B.Swarte,
K.H.Kalk,
W.G.Hol,
J.Drenth.
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Ref.
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Proteins, 1992,
14,
178-190.
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PubMed id
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Secondary reference #2
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Title
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The influence of purification and protein heterogeneity on the crystallization of p-Hydroxybenzoate hydroxylase.
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Authors
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J.M.Van der laan,
M.B.Swarte,
H.Groendijk,
W.G.Hol,
J.Drenth.
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Ref.
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Eur J Biochem, 1989,
179,
715-724.
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PubMed id
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Secondary reference #3
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Title
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The coenzyme analogue adenosine 5-Diphosphoribose displaces FAD in the active site of p-Hydroxybenzoate hydroxylase. An x-Ray crystallographic investigation.
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Authors
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J.M.Van der laan,
H.A.Schreuder,
M.B.Swarte,
R.K.Wierenga,
K.H.Kalk,
W.G.Hol,
J.Drenth.
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Ref.
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Biochemistry, 1989,
28,
7199-7205.
[DOI no: ]
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PubMed id
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Secondary reference #4
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Title
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Analysis of the active site of the flavoprotein p-Hydroxybenzoate hydroxylase and some ideas with respect to its reaction mechanism.
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Authors
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H.A.Schreuder,
W.G.Hol,
J.Drenth.
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Ref.
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Biochemistry, 1990,
29,
3101-3108.
[DOI no: ]
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PubMed id
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Secondary reference #5
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Title
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Crystal structure of the p-Hydroxybenzoate hydroxylase-Substrate complex refined at 1.9 a resolution. Analysis of the enzyme-Substrate and enzyme-Product complexes.
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Authors
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H.A.Schreuder,
P.A.Prick,
R.K.Wierenga,
G.Vriend,
K.S.Wilson,
W.G.Hol,
J.Drenth.
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Ref.
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J Mol Biol, 1989,
208,
679-696.
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PubMed id
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Secondary reference #6
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Title
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Molecular modeling reveals the possible importance of a carbonyl oxygen binding pocket for the catalytic mechanism of p-Hydroxybenzoate hydroxylase.
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Authors
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H.A.Schreuder,
W.G.Hol,
J.Drenth.
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Ref.
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J Biol Chem, 1988,
263,
3131-3136.
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PubMed id
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Secondary reference #7
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Title
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Crystal structure of p-Hydroxybenzoate hydroxylase complexed with its reaction product 3,4-Dihydroxybenzoate.
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Authors
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H.A.Schreuder,
J.M.Van der laan,
W.G.Hol,
J.Drenth.
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Ref.
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J Mol Biol, 1988,
199,
637-648.
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PubMed id
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Secondary reference #8
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Title
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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.
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Authors
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R.K.Wierenga,
J.Drenth,
G.E.Schulz.
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Ref.
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J Mol Biol, 1983,
167,
725-739.
[DOI no: ]
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PubMed id
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Figure 2.
FIG. 2. Superposition of the FAD-binding domains of (residues l to 163, thick lines) and
GRase (residues 8 to 159, thin lines, several residues labeled, residues 51 and 52 are behind the
adenine) together with the bound FAD molecules. For clarity only the C= atoms and the virtual =-C=
bonds of the polypeptide chain are drawn out. Th superposition is based on the minimal
distance between 69 C= atoms tht are mostly in fl-sheet strands and in helix ~A. These C= atoms ar
marked in Table l, which also gives the equivalencin scheme. The resulting r.m.s, distance btween
these 69 C= atoms is 1 '2 ~,.
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Figure 4.
FIG. 4. Superposition of ~Aa~fls units together with the FAD molecules. Shown are residues 1 to 45
of p-HBHase (thick lines) and residues 19 to 63 of GRase (thin lines, several residues labeled). The
polypeptide chain is reduced to the virtual C=-C= bonds. The superposition is based on the minimal
r.m.s, distance btween the C= atoms of rsidues 2 to 34 of p-HBHase and residues 20 to 52 of GRase
as well as between 27 of the 53 non-hydrogen atoms of FAD distributed uniformly over the FAD
molecules. The resulting r.m.s, distance between these 33 C= atoms is 12 A and the r.m.s, distance
between all 53 FAD atoms is 1-1 A. The viewing irection is similar to Fig. 2.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #9
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Title
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Crystal structure of p-Hydroxybenzoate hydroxylase.
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Authors
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R.K.Wierenga,
R.J.De jong,
K.H.Kalk,
W.G.Hol,
J.Drenth.
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Ref.
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J Mol Biol, 1979,
131,
55-73.
[DOI no: ]
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PubMed id
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Figure 3.
FIG. 3. The secondary structure of p-OHbz hydroxylase. llBFE indicates the orientation with
respect to Fig. 1. The crystallographic 2.fold axis is indicated. Although not clear from this
diagram, sitlc-chains of H5 ir&ract with side-chaims of Hl. The orientation of FAD is indicated
by 1'1 (isoalloxazie ring), by I' (the phosphate groups) and by Ad (the adenine ring). The gold
(NaAu(CN),) position lia marked by an asterisk. The broken lines delineate the 3 domains. + or
indicate that t,he N-terminal end or the C-terminal end of a /3-strand points to the viewer.
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Figure 10.
FIG. 10. Structure of the oxidized form of the isoalloxazinn ring. The two nitrugen-containing
aromatic rings form the pteridine skeleton.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #10
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Title
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Crystallization and preliminary X-Ray investigation of p-Hydroxybenzoate hydroxylase from pseudomonas fluorescens.
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Authors
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J.Drenth,
W.G.Hol,
R.K.Wierenga.
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Ref.
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J Biol Chem, 1975,
250,
5268-5269.
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PubMed id
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