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PDBsum entry 1jax
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Structural genomics
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PDB id
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1jax
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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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Structures of f420h2:NADP+ oxidoreductase with and without its substrates bound.
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Authors
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E.Warkentin,
B.Mamat,
M.Sordel-Klippert,
M.Wicke,
R.K.Thauer,
M.Iwata,
S.Iwata,
U.Ermler,
S.Shima.
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Ref.
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EMBO J, 2001,
20,
6561-6569.
[DOI no: ]
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PubMed id
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Abstract
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Cofactor F420 is a 5'-deazaflavin derivative first discovered in methanogenic
archaea but later found also to be present in some bacteria. As a coenzyme, it
is involved in hydride transfer reactions and as a prosthetic group in the DNA
photolyase reaction. We report here for the first time on the crystal structure
of an F420-dependent oxidoreductase bound with F420. The structure of
F420H2:NADP+ oxidoreductase resolved to 1.65 A contains two domains: an
N-terminal domain characteristic of a dinucleotide-binding Rossmann fold and a
smaller C-terminal domain. The nicotinamide and the deazaflavin part of the two
coenzymes are bound in the cleft between the domains such that the Si-faces of
both face each other at a distance of 3.1 A, which is optimal for hydride
transfer. Comparison of the structures bound with and without substrates reveals
that of the two substrates NADP has to bind first, the binding being associated
with an induced fit.
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Figure 1.
Figure 1 Reaction catalysed by F[420]H[2]:NADP+ oxidoreductase.
The Re-faces of the cofactors are shown. The amide group of NADP
is shown in the trans conformation.
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Figure 4.
Figure 4 Stereo diagram of the active site of Fno. The
nicotinamide ring of NADP+ and the deazaflavin ring of F[420]
are embedded face on face in the hydrophobic pocket.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
6561-6569)
copyright 2001.
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