| pubmed-article:17481658 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17481658 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:17481658 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:17481658 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17481658 | lifeskim:mentions | umls-concept:C1523987 | lld:lifeskim |
| pubmed-article:17481658 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:17481658 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:17481658 | pubmed:dateCreated | 2007-5-21 | lld:pubmed |
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| pubmed-article:17481658 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17481658 | pubmed:abstractText | The sigma subunit of bacterial RNA polymerase (RNAP) regulates gene expression by directing RNAP to specific promoters. Unlike sigma(70)-type proteins, the alternative sigma factor, sigma(54), requires interaction with an ATPase to open DNA. We present the solution structure of the C-terminal domain of sigma(54) bound to the -24 promoter element, in which the conserved RpoN box motif inserts into the major groove of the DNA. This structure elucidates the basis for sequence specific recognition of the -24 element, orients sigma(54) on the promoter, and suggests how the C-terminal domain of sigma(54) interacts with RNAP. | lld:pubmed |
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| pubmed-article:17481658 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17481658 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17481658 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17481658 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17481658 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17481658 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:17481658 | pubmed:author | pubmed-author:WemmerDavid... | lld:pubmed |
| pubmed-article:17481658 | pubmed:author | pubmed-author:NixonB... | lld:pubmed |
| pubmed-article:17481658 | pubmed:author | pubmed-author:DoucleffMicha... | lld:pubmed |
| pubmed-article:17481658 | pubmed:author | pubmed-author:PeltonJeffrey... | lld:pubmed |
| pubmed-article:17481658 | pubmed:author | pubmed-author:LeePeter SPS | lld:pubmed |
| pubmed-article:17481658 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17481658 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17481658 | pubmed:volume | 369 | lld:pubmed |
| pubmed-article:17481658 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17481658 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17481658 | pubmed:pagination | 1070-8 | lld:pubmed |
| pubmed-article:17481658 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17481658 | pubmed:meshHeading | pubmed-meshheading:17481658... | lld:pubmed |
| pubmed-article:17481658 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17481658 | pubmed:articleTitle | Structural basis of DNA recognition by the alternative sigma-factor, sigma54. | lld:pubmed |
| pubmed-article:17481658 | pubmed:affiliation | Physical Biosciences Division, Lawrence Berkeley National Laboratory and the Department of Chemistry, University of California, Berkeley, CA 94720, USA. | lld:pubmed |
| pubmed-article:17481658 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17481658 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:17481658 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17481658 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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