| pubmed-article:20541511 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20541511 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:20541511 | lifeskim:mentions | umls-concept:C0012906 | lld:lifeskim |
| pubmed-article:20541511 | lifeskim:mentions | umls-concept:C2700116 | lld:lifeskim |
| pubmed-article:20541511 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:20541511 | lifeskim:mentions | umls-concept:C0332453 | lld:lifeskim |
| pubmed-article:20541511 | lifeskim:mentions | umls-concept:C0115886 | lld:lifeskim |
| pubmed-article:20541511 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:20541511 | pubmed:dateCreated | 2010-6-14 | lld:pubmed |
| pubmed-article:20541511 | pubmed:abstractText | The crystal structure of the rare-cutting HNH restriction endonuclease PacI in complex with its eight-base-pair target recognition sequence 5'-TTAATTAA-3' has been determined to 1.9 A resolution. The enzyme forms an extended homodimer, with each subunit containing two zinc-bound motifs surrounding a betabetaalpha-metal catalytic site. The latter is unusual in that a tyrosine residue likely initiates strand cleavage. PacI dramatically distorts its target sequence from Watson-Crick duplex DNA base pairing, with every base separated from its original partner. Two bases on each strand are unpaired, four are engaged in noncanonical A:A and T:T base pairs, and the remaining two bases are matched with new Watson-Crick partners. This represents a highly unusual DNA binding mechanism for a restriction endonuclease, and implies that initial recognition of the target site might involve significantly different contacts from those visualized in the DNA-bound cocrystal structures. | lld:pubmed |
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| pubmed-article:20541511 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20541511 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20541511 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20541511 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20541511 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:20541511 | pubmed:issn | 1878-4186 | lld:pubmed |
| pubmed-article:20541511 | pubmed:author | pubmed-author:MorganRichard... | lld:pubmed |
| pubmed-article:20541511 | pubmed:author | pubmed-author:WangHuaH | lld:pubmed |
| pubmed-article:20541511 | pubmed:author | pubmed-author:StoddardBarry... | lld:pubmed |
| pubmed-article:20541511 | pubmed:author | pubmed-author:WilsonGeoffre... | lld:pubmed |
| pubmed-article:20541511 | pubmed:author | pubmed-author:XuShuang-Yong... | lld:pubmed |
| pubmed-article:20541511 | pubmed:author | pubmed-author:ChanSiu-HongS... | lld:pubmed |
| pubmed-article:20541511 | pubmed:author | pubmed-author:ShenBetty WBW | lld:pubmed |
| pubmed-article:20541511 | pubmed:author | pubmed-author:HeiterDaniel... | lld:pubmed |
| pubmed-article:20541511 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20541511 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:20541511 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:20541511 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20541511 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20541511 | pubmed:pagination | 734-43 | lld:pubmed |
| pubmed-article:20541511 | pubmed:dateRevised | 2011-11-7 | lld:pubmed |
| pubmed-article:20541511 | pubmed:meshHeading | pubmed-meshheading:20541511... | lld:pubmed |
| pubmed-article:20541511 | pubmed:meshHeading | pubmed-meshheading:20541511... | lld:pubmed |
| pubmed-article:20541511 | pubmed:meshHeading | pubmed-meshheading:20541511... | lld:pubmed |
| pubmed-article:20541511 | pubmed:meshHeading | pubmed-meshheading:20541511... | lld:pubmed |
| pubmed-article:20541511 | pubmed:meshHeading | pubmed-meshheading:20541511... | lld:pubmed |
| pubmed-article:20541511 | pubmed:meshHeading | pubmed-meshheading:20541511... | lld:pubmed |
| pubmed-article:20541511 | pubmed:meshHeading | pubmed-meshheading:20541511... | lld:pubmed |
| pubmed-article:20541511 | pubmed:meshHeading | pubmed-meshheading:20541511... | lld:pubmed |
| pubmed-article:20541511 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20541511 | pubmed:articleTitle | Unusual target site disruption by the rare-cutting HNH restriction endonuclease PacI. | lld:pubmed |
| pubmed-article:20541511 | pubmed:affiliation | Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue N. A3-025, Seattle, WA 98109, USA. | lld:pubmed |
| pubmed-article:20541511 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20541511 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20541511 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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