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PDBsum entry 1gw2
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Oxidoreductase
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PDB id
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1gw2
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Hrpc heme crevice architecture
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Authors
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A.Henriksen,
K.Meno,
N.Brissett,
M.Gajhede.
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Ref.
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To be Published ...
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Secondary reference #1
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Title
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The structures of the horseradish peroxidase c-Ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates.
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Authors
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A.Henriksen,
A.T.Smith,
M.Gajhede.
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Ref.
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J Biol Chem, 1999,
274,
35005-35011.
[DOI no: ]
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PubMed id
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Figure 2.
Fig. 2. A, the 1.5  simulated
anneal omit 2 F[o]  F[c]
density surrounding the cyanide and the water molecule in the
active site of the HRPC-CN-FA complex and the 0.3 simulated
anneal omit 2 F[o] F[c]
density surrounding FA molecules in the HRPC-CN-FA complex. B,
the active site of HRPC-CN-FA. Hydrogen bonds between active
site residues and ligands are indicated with dotted black lines.
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Figure 3.
Fig. 3. Proposed mechanism for substrate oxidation in
plant peroxidases. First, the active site arginine (Arg38 in
HRPC) donates a hydrogen bond to the phenolic oxygen of the
reducing substrate. This hydrogen bond will assist proton
transfer from the phenolic oxygen to active site histidine (His
42 in HRPC) through an active site water molecule held in
position by the backbone oxygen of a conserved proline residue
(Pro139 in HRPC). The electron is transferred to the heme group
via the C-18 methyl-C-20 heme edge. Then compound II reduction
is assisted by similar a proton transfer. The proton can be
transferred to the ferryl oxygen through the active site water
molecule situated equidistant between the distal histidine and
the expected position of the ferryl oxygen of compound II,
regenerating the resting state enzyme and a water molecule.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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Secondary reference #2
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Title
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Structural interactions between horseradish peroxidase c and the substrate benzhydroxamic acid determined by x-Ray crystallography.
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Authors
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A.Henriksen,
D.J.Schuller,
K.Meno,
K.G.Welinder,
A.T.Smith,
M.Gajhede.
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Ref.
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Biochemistry, 1998,
37,
8054-8060.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Crystal structure of horseradish peroxidase c at 2.15 a resolution.
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Authors
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M.Gajhede,
D.J.Schuller,
A.Henriksen,
A.T.Smith,
T.L.Poulos.
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Ref.
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Nat Struct Biol, 1997,
4,
1032-1038.
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PubMed id
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Secondary reference #4
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Title
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Crystallization and preliminary X-Ray studies of recombinant horseradish peroxidase.
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Authors
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A.Henriksen,
M.Gajhede,
P.Baker,
A.T.Smith,
J.F.Burke.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1995,
51,
121-123.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. HRPC* prisms of 0.3 x 0.3 x 0.2mm grown from 16%
PEG4000, 0.2 M zinc acetate and 0.1 M cacodylate buffer of pH 6.5.
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Figure 2.
Fig. 2. Diagram of the intensities at reciprocal lattice points in the
hkl
plane for data processed in space group P1. c* is normal to the plane
and b* is running horizontally from left to right. The diagram shows
threefold symmetry and mirror planes between the reciprocal axis.
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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