| pubmed-article:18321528 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18321528 | lifeskim:mentions | umls-concept:C0033809 | lld:lifeskim |
| pubmed-article:18321528 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18321528 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:18321528 | lifeskim:mentions | umls-concept:C1148846 | lld:lifeskim |
| pubmed-article:18321528 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:18321528 | pubmed:dateCreated | 2008-3-24 | lld:pubmed |
| pubmed-article:18321528 | pubmed:abstractText | Tex is a highly conserved bacterial protein that likely functions in a variety of transcriptional processes. Here, we describe two crystal structures of the 86-kDa Tex protein from Pseudomonas aeruginosa at 2.3 and 2.5 A resolution, respectively. These structures reveal a relatively flat and elongated protein, with several potential nucleic acid binding motifs clustered at one end, including an S1 domain near the C-terminus that displays considerable structural flexibility. Tex binds nucleic acids, with a preference for single-stranded RNA, and the Tex S1 domain is required for this binding activity. Point mutants further demonstrate that the primary nucleic acid binding site corresponds to a surface of the S1 domain. Sequence alignment and modeling indicate that the eukaryotic Spt6 transcription factor adopts a similar core structure. Structural analysis further suggests that the RNA polymerase and nucleosome interacting regions of Spt6 flank opposite sides of the Tex-like scaffold. Therefore, the Tex structure may represent a conserved scaffold that binds single-stranded RNA to regulate transcription in both eukaryotic and prokaryotic organisms. | lld:pubmed |
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| pubmed-article:18321528 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18321528 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18321528 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18321528 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18321528 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18321528 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18321528 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:18321528 | pubmed:issn | 1089-8638 | lld:pubmed |
| pubmed-article:18321528 | pubmed:author | pubmed-author:DoveSimon LSL | lld:pubmed |
| pubmed-article:18321528 | pubmed:author | pubmed-author:HillChristoph... | lld:pubmed |
| pubmed-article:18321528 | pubmed:author | pubmed-author:RobinsonHowar... | lld:pubmed |
| pubmed-article:18321528 | pubmed:author | pubmed-author:JohnsonSean... | lld:pubmed |
| pubmed-article:18321528 | pubmed:author | pubmed-author:Vallet-GelyIs... | lld:pubmed |
| pubmed-article:18321528 | pubmed:author | pubmed-author:CloseDevinD | lld:pubmed |
| pubmed-article:18321528 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18321528 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:18321528 | pubmed:volume | 377 | lld:pubmed |
| pubmed-article:18321528 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18321528 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18321528 | pubmed:pagination | 1460-73 | lld:pubmed |
| pubmed-article:18321528 | pubmed:dateRevised | 2010-12-17 | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:meshHeading | pubmed-meshheading:18321528... | lld:pubmed |
| pubmed-article:18321528 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18321528 | pubmed:articleTitle | Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. | lld:pubmed |
| pubmed-article:18321528 | pubmed:affiliation | Department of Chemistry and Biochemistry, Utah State University, Logan, UT 84322-0300, USA. | lld:pubmed |
| pubmed-article:18321528 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18321528 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
