| pubmed-article:20833632 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20833632 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:20833632 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:20833632 | lifeskim:mentions | umls-concept:C0014230 | lld:lifeskim |
| pubmed-article:20833632 | lifeskim:mentions | umls-concept:C0332514 | lld:lifeskim |
| pubmed-article:20833632 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:20833632 | pubmed:dateCreated | 2011-1-24 | lld:pubmed |
| pubmed-article:20833632 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20833632 | pubmed:abstractText | Restriction enzymes share little or no sequence homology with the exception of isoschizomers, or enzymes that recognize and cleave the same DNA sequence. We present here the structure of a BamHI isoschizomer, OkrAI, bound to the same DNA sequence (TATGGATCCATA) as that cocrystallized with BamHI. We show that OkrAI is a more minimal version of BamHI, lacking not only the N- and C-terminal helices but also an internal 3(10) helix and containing ?-strands that are shorter than those in BamHI. Despite these structural differences, OkrAI recognizes the DNA in a remarkably similar manner to BamHI, including asymmetric contacts via C-terminal 'arms' that appear to 'compete' for the minor groove. However, the arms are shorter than in BamHI. We observe similar DNA-binding affinities between OkrAI and BamHI but OkrAI has higher star activity (at 37°C) compared to BamHI. Together, the OkrAI and BamHI structures offer a rare opportunity to compare two restriction enzymes that work on exactly the same DNA substrate. | lld:pubmed |
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| pubmed-article:20833632 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20833632 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20833632 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20833632 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20833632 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20833632 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:20833632 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:20833632 | pubmed:author | pubmed-author:AggarwalAneel... | lld:pubmed |
| pubmed-article:20833632 | pubmed:author | pubmed-author:XuShuang-yong... | lld:pubmed |
| pubmed-article:20833632 | pubmed:author | pubmed-author:ViadiuHectorH | lld:pubmed |
| pubmed-article:20833632 | pubmed:author | pubmed-author:ChanSiu-HongS... | lld:pubmed |
| pubmed-article:20833632 | pubmed:author | pubmed-author:VanameeEva... | lld:pubmed |
| pubmed-article:20833632 | pubmed:author | pubmed-author:UmmatAjayA | lld:pubmed |
| pubmed-article:20833632 | pubmed:author | pubmed-author:HartlineAdria... | lld:pubmed |
| pubmed-article:20833632 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20833632 | pubmed:volume | 39 | lld:pubmed |
| pubmed-article:20833632 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20833632 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20833632 | pubmed:pagination | 712-9 | lld:pubmed |
| pubmed-article:20833632 | pubmed:dateRevised | 2011-7-20 | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:meshHeading | pubmed-meshheading:20833632... | lld:pubmed |
| pubmed-article:20833632 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:20833632 | pubmed:articleTitle | Asymmetric DNA recognition by the OkrAI endonuclease, an isoschizomer of BamHI. | lld:pubmed |
| pubmed-article:20833632 | pubmed:affiliation | Department of Structural and Chemical Biology, Mount Sinai School of Medicine, New York, NY 10029, USA. | lld:pubmed |
| pubmed-article:20833632 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20833632 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
