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| pubmed-article:10366505 | lifeskim:mentions | umls-concept:C0025831 | lld:lifeskim |
| pubmed-article:10366505 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:10366505 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:10366505 | lifeskim:mentions | umls-concept:C0178555 | lld:lifeskim |
| pubmed-article:10366505 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10366505 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:10366505 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:10366505 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10366505 | pubmed:dateCreated | 1999-7-12 | lld:pubmed |
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| pubmed-article:10366505 | pubmed:abstractText | The rRNA methyltransferase ErmC' transfers methyl groups from S -adenosyl-l-methionine to atom N6 of an adenine base within the peptidyltransferase loop of 23 S rRNA, thus conferring antibiotic resistance against a number of macrolide antibiotics. The crystal structures of ErmC' and of its complexes with the cofactor S -adenosyl-l-methionine, the reaction product S-adenosyl-l-homocysteine and the methyltransferase inhibitor Sinefungin, respectively, show that the enzyme undergoes small conformational changes upon ligand binding. Overall, the ligand molecules bind to the protein in a similar mode as observed for other methyltransferases. Small differences between the binding of the amino acid parts of the different ligands are correlated with differences in their chemical structure. A model for the transition-state based on the atomic details of the active site is consistent with a one-step methyl-transfer mechanism and might serve as a first step towards the design of potent Erm inhibitors. | lld:pubmed |
| pubmed-article:10366505 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10366505 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10366505 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10366505 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10366505 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10366505 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:10366505 | pubmed:author | pubmed-author:Abad-Zapatero... | lld:pubmed |
| pubmed-article:10366505 | pubmed:author | pubmed-author:StewartK DKD | lld:pubmed |
| pubmed-article:10366505 | pubmed:author | pubmed-author:ZhongPP | lld:pubmed |
| pubmed-article:10366505 | pubmed:author | pubmed-author:KavanaughT... | lld:pubmed |
| pubmed-article:10366505 | pubmed:author | pubmed-author:SchluckebierG... | lld:pubmed |
| pubmed-article:10366505 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10366505 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10366505 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:10366505 | pubmed:volume | 289 | lld:pubmed |
| pubmed-article:10366505 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10366505 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10366505 | pubmed:pagination | 277-91 | lld:pubmed |
| pubmed-article:10366505 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10366505 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10366505 | pubmed:articleTitle | The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism. | lld:pubmed |
| pubmed-article:10366505 | pubmed:affiliation | Abbott Laboratories, D46Y-AP 10, 100 Abbott Park Road, Abbott Park, IL, 60064, USA. gerd.schluckebier@abbott.com | lld:pubmed |
| pubmed-article:10366505 | pubmed:publicationType | Journal Article | lld:pubmed |
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