| pubmed-article:17618295 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17618295 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:17618295 | lifeskim:mentions | umls-concept:C0547040 | lld:lifeskim |
| pubmed-article:17618295 | lifeskim:mentions | umls-concept:C0208356 | lld:lifeskim |
| pubmed-article:17618295 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17618295 | lifeskim:mentions | umls-concept:C1514185 | lld:lifeskim |
| pubmed-article:17618295 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:17618295 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:17618295 | pubmed:dateCreated | 2007-8-6 | lld:pubmed |
| pubmed-article:17618295 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17618295 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17618295 | pubmed:abstractText | Chlorella virus DNA ligase, the smallest eukaryotic ligase known, has pluripotent biological activity and an intrinsic nick-sensing function, despite having none of the accessory domains found in cellular ligases. A 2.3-A crystal structure of the Chlorella virus ligase-AMP intermediate bound to duplex DNA containing a 3'-OH-5'-PO4 nick reveals a new mode of DNA envelopment, in which a short surface loop emanating from the OB domain forms a beta-hairpin 'latch' that inserts into the DNA major groove flanking the nick. A network of interactions with the 3'-OH and 5'-PO4 termini in the active site illuminates the DNA adenylylation mechanism and the crucial roles of AMP in nick sensing and catalysis. Addition of a divalent cation triggered nick sealing in crystallo, establishing that the nick complex is a bona fide intermediate in the DNA repair pathway. | lld:pubmed |
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| pubmed-article:17618295 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17618295 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17618295 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17618295 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17618295 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17618295 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:17618295 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:17618295 | pubmed:author | pubmed-author:ShumanStewart... | lld:pubmed |
| pubmed-article:17618295 | pubmed:author | pubmed-author:LimaChristoph... | lld:pubmed |
| pubmed-article:17618295 | pubmed:author | pubmed-author:SmithPaulP | lld:pubmed |
| pubmed-article:17618295 | pubmed:author | pubmed-author:OdellMarkM | lld:pubmed |
| pubmed-article:17618295 | pubmed:author | pubmed-author:NandakumarJay... | lld:pubmed |
| pubmed-article:17618295 | pubmed:author | pubmed-author:NairPravin... | lld:pubmed |
| pubmed-article:17618295 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17618295 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:17618295 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17618295 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17618295 | pubmed:pagination | 770-8 | lld:pubmed |
| pubmed-article:17618295 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
| pubmed-article:17618295 | pubmed:meshHeading | pubmed-meshheading:17618295... | lld:pubmed |
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| pubmed-article:17618295 | pubmed:meshHeading | pubmed-meshheading:17618295... | lld:pubmed |
| pubmed-article:17618295 | pubmed:meshHeading | pubmed-meshheading:17618295... | lld:pubmed |
| pubmed-article:17618295 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17618295 | pubmed:articleTitle | Structural basis for nick recognition by a minimal pluripotent DNA ligase. | lld:pubmed |
| pubmed-article:17618295 | pubmed:affiliation | Molecular Biology and Structural Biology Programs, Sloan-Kettering Institute, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:17618295 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17618295 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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