| pubmed-article:15235592 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15235592 | lifeskim:mentions | umls-concept:C0010851 | lld:lifeskim |
| pubmed-article:15235592 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:15235592 | lifeskim:mentions | umls-concept:C1419240 | lld:lifeskim |
| pubmed-article:15235592 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:15235592 | pubmed:dateCreated | 2004-7-28 | lld:pubmed |
| pubmed-article:15235592 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:abstractText | Rad51, the major eukaryotic homologous recombinase, is important for the repair of DNA damage and the maintenance of genomic diversity and stability. The active form of this DNA-dependent ATPase is a helical filament within which the search for homology and strand exchange occurs. Here we present the crystal structure of a Saccharomyces cerevisiae Rad51 filament formed by a gain-of-function mutant. This filament has a longer pitch than that seen in crystals of Rad51's prokaryotic homolog RecA, and places the ATPase site directly at a new interface between protomers. Although the filament exhibits approximate six-fold symmetry, alternate protein-protein interfaces are slightly different, implying that the functional unit of Rad51 within the filament may be a dimer. Additionally, we show that mutation of His352, which lies at this new interface, markedly disrupts DNA binding. | lld:pubmed |
| pubmed-article:15235592 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15235592 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15235592 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15235592 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15235592 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:15235592 | pubmed:author | pubmed-author:LynchThomas... | lld:pubmed |
| pubmed-article:15235592 | pubmed:author | pubmed-author:ZhangYingY | lld:pubmed |
| pubmed-article:15235592 | pubmed:author | pubmed-author:FortinGary... | lld:pubmed |
| pubmed-article:15235592 | pubmed:author | pubmed-author:SymingtonLorr... | lld:pubmed |
| pubmed-article:15235592 | pubmed:author | pubmed-author:ConwayAdam... | lld:pubmed |
| pubmed-article:15235592 | pubmed:author | pubmed-author:RicePhoebe... | lld:pubmed |
| pubmed-article:15235592 | pubmed:author | pubmed-author:FungCindy WCW | lld:pubmed |
| pubmed-article:15235592 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15235592 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:15235592 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15235592 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15235592 | pubmed:pagination | 791-6 | lld:pubmed |
| pubmed-article:15235592 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15235592 | pubmed:meshHeading | pubmed-meshheading:15235592... | lld:pubmed |
| pubmed-article:15235592 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15235592 | pubmed:articleTitle | Crystal structure of a Rad51 filament. | lld:pubmed |
| pubmed-article:15235592 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, The University of Chicago, 920 East 58th Street, Chicago, Illinois 60637, USA. | lld:pubmed |
| pubmed-article:15235592 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15235592 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15235592 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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