Linked Life Data

15576622

Source:http://linkedlifedata.com/resource/pubmed/id/15576622

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5702
pubmed:dateCreated
2004-12-3
pubmed:databankReference
pubmed:abstractText
DNA photolyases use light energy to repair DNA that comprises ultraviolet-induced lesions such as the cis-syn cyclobutane pyrimidine dimers (CPDs). Here we report the crystal structure of a DNA photolyase bound to duplex DNA that is bent by 50 degrees and comprises a synthetic CPD lesion. This CPD lesion is flipped into the active site and split there into two thymines by synchrotron radiation at 100 K. Although photolyases catalyze blue light-driven CPD cleavage only above 200 K, this structure apparently mimics a structural substate during light-driven DNA repair in which back-flipping of the thymines into duplex DNA has not yet taken place.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
3
pubmed:volume
306
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1789-93
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair.
pubmed:affiliation
Department of Chemistry and Biochemistry, Butenandt-Strasse 5-13, Ludwig Maximilians University, D-81377 Munich, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't