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PDBsum entry 1vlf
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Oxidoreductase
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PDB id
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1vlf
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Contents |
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(+ 0 more)
875 a.a.
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(+ 0 more)
274 a.a.
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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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Crystal structure of pyrogallol-Phloroglucinol transhydroxylase, An mo enzyme capable of intermolecular hydroxyl transfer between phenols.
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Authors
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A.Messerschmidt,
H.Niessen,
D.Abt,
O.Einsle,
B.Schink,
P.M.Kroneck.
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Ref.
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Proc Natl Acad Sci U S A, 2004,
101,
11571-11576.
[DOI no: ]
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PubMed id
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Abstract
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The Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter
acidigallici catalyzes the conversion of pyrogallol to phloroglucinol. Such
trihydroxybenzenes and their derivatives represent important building blocks of
plant polymers. None of the transferred hydroxyl groups originates from water
during transhydroxylation; instead a cosubstrate, such as
1,2,3,5-tetrahydroxybenzene, is used in a reaction without apparent electron
transfer. Here, we report on the crystal structure of the enzyme in the reduced
Mo(IV) state, which we solved by single anomalous-diffraction technique. It
represents the largest structure (1,149 amino acid residues per molecule, 12
independent molecules per unit cell), which has been solved so far by single
anomalous-diffraction technique. Tranhydroxylase is a heterodimer, with the
active Mo-molybdopterin guanine dinucleotide (MGD)(2) site in the alpha-subunit,
and three [4Fe-4S] centers in the beta-subunit. The latter subunit carries a
seven-stranded, mainly antiparallel beta-barrel domain. We propose a scheme for
the transhydroxylation reaction based on 3D structures of complexes of the
enzyme with various polyphenols serving either as substrate or inhibitor.
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Figure 1.
Fig. 1. Overall structure of TH. The  -subunit domains I-IV
are shown in magenta, blue, red, and cream, respectively. The
 -subunit domains I and
II are shown in orange and pink, respectively, and domain III is
shown in green. The Mo and MGD cofactors are shown as
ball-and-stick models, and the three [4Fe--4S] clusters are
shown as red (Fe) and yellow (S) spheres. The figure was made
with BOBSCRIPT (31) and RASTER3D (32).
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Figure 2.
Fig. 2. Solid-surface-electrostatic potential
representation of TH displaying the access channel for substrate
and cosubstrate. The electrostatic surface potentials are
contoured from -10 (red) to 10 K[B]T/e (blue). The figure was
made with GRASP (34) and RASTER3D (32).
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