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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-4-15
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pubmed:databankReference |
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pubmed:abstractText |
DNA ligases catalyse phosphodiester bond formation between adjacent bases in nicked DNA, thereby sealing the nick. A key step in the catalytic mechanism is the formation of an adenylated DNA intermediate. The adenyl group is derived from either ATP (in eucaryotes and archaea) or NAD+4 (in bacteria). This difference in cofactor specificity suggests that DNA ligase may be a useful antibiotic target.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35-42
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10368271-Adenosine Triphosphate,
pubmed-meshheading:10368271-Amino Acid Sequence,
pubmed-meshheading:10368271-Binding Sites,
pubmed-meshheading:10368271-Cloning, Molecular,
pubmed-meshheading:10368271-Crystallography, X-Ray,
pubmed-meshheading:10368271-DNA Ligases,
pubmed-meshheading:10368271-Geobacillus stearothermophilus,
pubmed-meshheading:10368271-Models, Molecular,
pubmed-meshheading:10368271-Molecular Sequence Data,
pubmed-meshheading:10368271-NAD,
pubmed-meshheading:10368271-Protein Folding,
pubmed-meshheading:10368271-Protein Structure, Secondary,
pubmed-meshheading:10368271-Recombinant Proteins,
pubmed-meshheading:10368271-Sequence Alignment,
pubmed-meshheading:10368271-Sequence Homology, Amino Acid,
pubmed-meshheading:10368271-Substrate Specificity
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pubmed:year |
1999
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pubmed:articleTitle |
Structure of the adenylation domain of an NAD+-dependent DNA ligase.
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pubmed:affiliation |
Sir William Dunn School of Pathology, University of Oxford, South ParksRoad, Oxford OX1 3RE, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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