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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5219
|
| pubmed:dateCreated |
1995-8-7
|
| pubmed:abstractText |
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.
|
| pubmed:grant | |
| pubmed:commentsCorrections | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/5,11-methenyltetrahydrohomofolate,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribodipyrimidine Photo-Lyase,
http://linkedlifedata.com/resource/pubmed/chemical/Flavin-Adenine Dinucleotide,
http://linkedlifedata.com/resource/pubmed/chemical/Folic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrimidine Dimers
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0036-8075
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
30
|
| pubmed:volume |
268
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1866-72
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7604260-Amino Acid Sequence,
pubmed-meshheading:7604260-Computer Graphics,
pubmed-meshheading:7604260-Crystallography, X-Ray,
pubmed-meshheading:7604260-DNA, Bacterial,
pubmed-meshheading:7604260-DNA Damage,
pubmed-meshheading:7604260-DNA Repair,
pubmed-meshheading:7604260-Deoxyribodipyrimidine Photo-Lyase,
pubmed-meshheading:7604260-Electron Transport,
pubmed-meshheading:7604260-Escherichia coli,
pubmed-meshheading:7604260-Flavin-Adenine Dinucleotide,
pubmed-meshheading:7604260-Folic Acid,
pubmed-meshheading:7604260-Hydrogen Bonding,
pubmed-meshheading:7604260-Models, Molecular,
pubmed-meshheading:7604260-Molecular Sequence Data,
pubmed-meshheading:7604260-Protein Conformation,
pubmed-meshheading:7604260-Protein Folding,
pubmed-meshheading:7604260-Protein Structure, Secondary,
pubmed-meshheading:7604260-Protein Structure, Tertiary,
pubmed-meshheading:7604260-Pyrimidine Dimers
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Crystal structure of DNA photolyase from Escherichia coli.
|
| pubmed:affiliation |
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|