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PDBsum entry 1dnp
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Lyase (carbon-carbon)
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PDB id
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1dnp
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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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Crystal structure of DNA photolyase from escherichia coli.
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Authors
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H.W.Park,
S.T.Kim,
A.Sancar,
J.Deisenhofer.
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Ref.
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Science, 1995,
268,
1866-1872.
[DOI no: ]
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PubMed id
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Abstract
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Photolyase repairs ultraviolet (UV) damage to DNA by splitting the cyclobutane
ring of the major UV photoproduct, the cis, syn-cyclobutane pyrimidine dimer
(Pyr <> Pyr). The reaction is initiated by blue light and proceeds through
long-range energy transfer, single electron transfer, and enzyme catalysis by a
radical mechanism. The three-dimensional crystallographic structure of DNA
photolyase from Escherichia coli is presented and the atomic model was refined
to an R value of 0.172 at 2.3 A resolution. The polypeptide chain of 471 amino
acids is folded into an amino-terminal alpha/beta domain resembling dinucleotide
binding domains and a carboxyl-terminal helical domain; a loop of 72 residues
connects the domains. The light-harvesting cofactor
5,10-methenyltetrahydrofolylpolyglutamate (MTHF) binds in a cleft between the
two domains. Energy transfer from MTHF to the catalytic cofactor flavin adenine
dinucleotide (FAD) occurs over a distance of 16.8 A. The FAD adopts a U-shaped
conformation between two helix clusters in the center of the helical domain and
is accessible through a hole in the surface of this domain. Dimensions and
polarity of the hole match those of a Pyr <> Pyr dinucleotide, suggesting
that the Pyr <> Pyr "flips out" of the helix to fit into this hole,
and that electron transfer between the flavin and the Pyr <> Pyr occurs over
van der Waals contact distance.
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Secondary reference #1
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Title
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Crystallization and preliminary crystallographic analysis of escherichia coli DNA photolyase.
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Authors
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H.W.Park,
A.Sancar,
J.Deisenhofer.
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Ref.
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J Mol Biol, 1993,
231,
1122-1125.
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PubMed id
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