| pubmed-article:9628482 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9628482 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:9628482 | lifeskim:mentions | umls-concept:C0008018 | lld:lifeskim |
| pubmed-article:9628482 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:9628482 | lifeskim:mentions | umls-concept:C0033649 | lld:lifeskim |
| pubmed-article:9628482 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:9628482 | pubmed:dateCreated | 1998-6-30 | lld:pubmed |
| pubmed-article:9628482 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9628482 | pubmed:abstractText | Signal transduction processes commonly involve reversible covalent modifications of receptors. Bacterial chemotaxis receptors are reversibly methylated at specific glutamate residues within coiled-coil regions of their cytoplasmic domains. Methylation is catalyzed by an S-adenosylmethionine-dependent protein methyltransferase, CheR, that binds to a specific sequence at the C-termini of some chemotaxis receptors. From this tethering point, CheR methylates neighboring receptor molecules. We report the crystal structure, determined to 2.2 A resolution, of a complex of the Salmonella typhimurium methyltransferase CheR bound to the methylation reaction product, S-adenosylhomocysteine (AdoHcy), and the C-terminal pentapeptide of the aspartate receptor, Tar. The structure indicates the basis for the specificity of interaction between the chemoreceptors and CheR and identifies a specific receptor binding motif incorporated in the CheR methyltransferase domain. | lld:pubmed |
| pubmed-article:9628482 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9628482 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9628482 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9628482 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9628482 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9628482 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:9628482 | pubmed:author | pubmed-author:StockA MAM | lld:pubmed |
| pubmed-article:9628482 | pubmed:author | pubmed-author:DjordjevicSS | lld:pubmed |
| pubmed-article:9628482 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9628482 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:9628482 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9628482 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9628482 | pubmed:pagination | 446-50 | lld:pubmed |
| pubmed-article:9628482 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:9628482 | pubmed:meshHeading | pubmed-meshheading:9628482-... | lld:pubmed |
| pubmed-article:9628482 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9628482 | pubmed:articleTitle | Chemotaxis receptor recognition by protein methyltransferase CheR. | lld:pubmed |
| pubmed-article:9628482 | pubmed:affiliation | Howard Hughes Medical Institute, Center for Advanced Biotechnology and Medicine, and Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Piscataway 08854-5638, USA. | lld:pubmed |
| pubmed-article:9628482 | pubmed:publicationType | Journal Article | lld:pubmed |
| literatureCitation:4331_962... | literatureCitation:pubmed | pubmed-article:9628482 | lld:drugbank |
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