| pubmed-article:15135053 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C0035711 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C1537998 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C0441587 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C0332462 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15135053 | lifeskim:mentions | umls-concept:C2606649 | lld:lifeskim |
| pubmed-article:15135053 | pubmed:issue | 1-3 | lld:pubmed |
| pubmed-article:15135053 | pubmed:dateCreated | 2004-5-11 | lld:pubmed |
| pubmed-article:15135053 | pubmed:abstractText | Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine in structural RNA. The pseudouridine synthase TruD, that modifies U13 in tRNA, belongs to a recently identified and large family of pseudouridine synthases present in all kingdoms of life. We report here the crystal structure of Escherichia coli TruD at 2.0 A resolution. The structure reveals an overall V-shaped molecule with an RNA-binding cleft formed between two domains: a catalytic domain and an insertion domain. The catalytic domain has a fold similar to that of the catalytic domains of previously characterised pseudouridine synthases, whereas the insertion domain displays a novel fold. | lld:pubmed |
| pubmed-article:15135053 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15135053 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15135053 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15135053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15135053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15135053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15135053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15135053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15135053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15135053 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15135053 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15135053 | pubmed:month | May | lld:pubmed |
| pubmed-article:15135053 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:15135053 | pubmed:author | pubmed-author:NordlundPärP | lld:pubmed |
| pubmed-article:15135053 | pubmed:author | pubmed-author:HallbergB... | lld:pubmed |
| pubmed-article:15135053 | pubmed:author | pubmed-author:EricssonUlrik... | lld:pubmed |
| pubmed-article:15135053 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15135053 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:15135053 | pubmed:volume | 565 | lld:pubmed |
| pubmed-article:15135053 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15135053 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15135053 | pubmed:pagination | 59-64 | lld:pubmed |
| pubmed-article:15135053 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15135053 | pubmed:meshHeading | pubmed-meshheading:15135053... | lld:pubmed |
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| pubmed-article:15135053 | pubmed:meshHeading | pubmed-meshheading:15135053... | lld:pubmed |
| pubmed-article:15135053 | pubmed:meshHeading | pubmed-meshheading:15135053... | lld:pubmed |
| pubmed-article:15135053 | pubmed:meshHeading | pubmed-meshheading:15135053... | lld:pubmed |
| pubmed-article:15135053 | pubmed:meshHeading | pubmed-meshheading:15135053... | lld:pubmed |
| pubmed-article:15135053 | pubmed:meshHeading | pubmed-meshheading:15135053... | lld:pubmed |
| pubmed-article:15135053 | pubmed:meshHeading | pubmed-meshheading:15135053... | lld:pubmed |
| pubmed-article:15135053 | pubmed:meshHeading | pubmed-meshheading:15135053... | lld:pubmed |
| pubmed-article:15135053 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15135053 | pubmed:articleTitle | X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold. | lld:pubmed |
| pubmed-article:15135053 | pubmed:affiliation | Department of Biochemistry and Biophysics, Stockholm University, Roslagstullsbacken 15, SE-114 21 Stockholm, Sweden. | lld:pubmed |
| pubmed-article:15135053 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15135053 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947214 | entrezgene:pubmed | pubmed-article:15135053 | lld:entrezgene |
| family:PF01142.13 | family:pubmed | pubmed-article:15135053 | lld:pfam |
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