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| pubmed-article:11601846 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
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| pubmed-article:11601846 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:11601846 | lifeskim:mentions | umls-concept:C1744318 | lld:lifeskim |
| pubmed-article:11601846 | lifeskim:mentions | umls-concept:C0527356 | lld:lifeskim |
| pubmed-article:11601846 | lifeskim:mentions | umls-concept:C0205144 | lld:lifeskim |
| pubmed-article:11601846 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11601846 | pubmed:dateCreated | 2001-10-16 | lld:pubmed |
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| pubmed-article:11601846 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11601846 | pubmed:abstractText | The crystal structure of a novel Cre-Lox synapse was solved using phases from multiple isomorphous replacement and anomalous scattering, and refined to 2.05 A resolution. In this complex, a symmetric protein trimer is bound to a Y-shaped three-way DNA junction, a marked departure from the pseudo-4-fold symmetrical tetramer associated with Cre-mediated LoxP recombination. The three-way DNA junction was accommodated by a simple kink without significant distortion of the adjoining DNA duplexes. Although the mean angle between DNA arms in the Y and X structures was similar, adjacent Cre trimer subunits rotated 29 degrees relative to those in the tetramers. This rotation was accommodated at the protein-protein and DNA-DNA interfaces by interactions that are "quasi-equivalent" to those in the tetramer, analogous to packing differences of chemically identical viral subunits at non-equivalent positions in icosahedral capsids. This structural quasi-equivalence extends to function as Cre can bind to, cleave and perform strand transfer with a three-way Lox substrate. The structure explains the dual recognition of three and four-way junctions by site-specific recombinases as being due to shared structural features between the differently branched substrates and plasticity of the protein-protein interfaces. To our knowledge, this is the first direct demonstration of quasi-equivalence in both the assembly and function of an oligomeric enzyme. | lld:pubmed |
| pubmed-article:11601846 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11601846 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11601846 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11601846 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11601846 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11601846 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:11601846 | pubmed:author | pubmed-author:ChuV CVC | lld:pubmed |
| pubmed-article:11601846 | pubmed:author | pubmed-author:BaldwinE PEP | lld:pubmed |
| pubmed-article:11601846 | pubmed:author | pubmed-author:MartinS SSS | lld:pubmed |
| pubmed-article:11601846 | pubmed:author | pubmed-author:WoodsK CKC | lld:pubmed |
| pubmed-article:11601846 | pubmed:copyrightInfo | Copyright 2001 Academic Press. | lld:pubmed |
| pubmed-article:11601846 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11601846 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:11601846 | pubmed:volume | 313 | lld:pubmed |
| pubmed-article:11601846 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11601846 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11601846 | pubmed:pagination | 49-69 | lld:pubmed |
| pubmed-article:11601846 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11601846 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11601846 | pubmed:articleTitle | Quasi-equivalence in site-specific recombinase structure and function: crystal structure and activity of trimeric Cre recombinase bound to a three-way Lox DNA junction. | lld:pubmed |
| pubmed-article:11601846 | pubmed:affiliation | Section of Molecular and Cellular Biology, University of California, Davis, 1 Shields Ave, Davis, CA 95616, USA. | lld:pubmed |
| pubmed-article:11601846 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11601846 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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