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PDBsum entry 1lua
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Oxidoreductase
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PDB id
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1lua
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References listed in PDB file
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Key reference
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Title
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Structure of methylene-Tetrahydromethanopterin dehydrogenase from methylobacterium extorquens am1.
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Authors
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U.Ermler,
C.H.Hagemeier,
A.Roth,
U.Demmer,
W.Grabarse,
E.Warkentin,
J.A.Vorholt.
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Ref.
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Structure, 2002,
10,
1127-1137.
[DOI no: ]
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PubMed id
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Abstract
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NADP-dependent methylene-H(4)MPT dehydrogenase, MtdA, from Methylobacterium
extorquens AM1 catalyzes the dehydrogenation of
methylene-tetrahydromethanopterin and methylene-tetrahydrofolate with NADP(+) as
cosubstrate. The X-ray structure of MtdA with and without NADP bound was
established at 1.9 A resolution. The enzyme is present as a homotrimer. The
alpha,beta fold of the monomer is related to that of methylene-H(4)F
dehydrogenases, suggesting a common evolutionary origin. The position of the
active site is located within a large crevice built up by the two domains of one
subunit and one domain of a second subunit. Methylene-H(4)MPT could be modeled
into the cleft, and crucial active site residues such as Phe18, Lys256, His260,
and Thr102 were identified. The molecular basis of the different substrate
specificities and different catalytic demands of MtdA compared to
methylene-H(4)F dehydrogenases are discussed.
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Figure 1.
Figure 1. Reaction of MtdAMethylene-H[4]MPT (-H[4]F) is
oxidized to methenyl-H[4]MPT (-H[4]F) with NADP+ as cosubstrate.
H[4]MPT is composed of a 7-methyl-6-ethyl-pterin, an
aminobenzyl, a 1-desoxyribose, a ribose, a phosphate, and a
2-hydroxyglutarate moiety. H[4]F consists of a 6-methyl-pterin,
a p-aminobenzoate, and a glutamate moiety. The two methyl groups
painted in blue are only present in H[4]MPT. Methylene and
methenyl groups are indicated in red.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
1127-1137)
copyright 2002.
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Secondary reference #1
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Title
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The NADP-Dependent methylene tetrahydromethanopterin dehydrogenase in methylobacterium extorquens am1.
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Authors
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J.A.Vorholt,
L.Chistoserdova,
M.E.Lidstrom,
R.K.Thauer.
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Ref.
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J Bacteriol, 1998,
180,
5351-5356.
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PubMed id
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