| pubmed-article:16793063 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C0165991 | lld:lifeskim |
| pubmed-article:16793063 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:16793063 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16793063 | pubmed:dateCreated | 2006-7-10 | lld:pubmed |
| pubmed-article:16793063 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16793063 | pubmed:abstractText | Nucleotide methylations are the most common type of rRNA modification in bacteria, and are introduced post-transcriptionally by a wide variety of site-specific enzymes. Three 5-methylcytidine (m(5)C) bases are found in the rRNAs of Escherichia coli and one of these, at nucleotide 1407 in 16 S rRNA, is the modification product of the methyltransferase (MTase) YebU (also called RsmF). YebU requires S-adenosyl-l-methionine (SAM) and methylates C1407 within assembled 30 S subunits, but not in naked 16 S rRNA or within tight-couple 70 S ribosomes. Here, we describe the three-dimensional structure of YebU determined by X-ray crystallography, and we present a molecular model for how YebU specifically recognizes, binds and methylates its ribosomal substrate. The YebU protein has an N-terminal SAM-binding catalytic domain with structural similarity to the equivalent domains in several other m(5)C RNA MTases including RsmB and PH1374. The C-terminal one-third of YebU contains a domain similar to that in pseudouridine synthases and archaeosine-specific transglycosylases (PUA-domain), which was not predicted by sequence alignments. Furthermore, YebU is predicted to contain extended regions of positive electrostatic potential that differ from other RNA-MTase structures, suggesting that YebU interacts with its RNA target in a different manner. Docking of YebU onto the 30 S subunit indicates that the PUA and MTase domains make several contacts with 16 S rRNA as well as with the ribosomal protein S12. The ribosomal protein interactions would explain why the assembled 30 S subunit, and not naked 16 S rRNA, is the preferred substrate for YebU. | lld:pubmed |
| pubmed-article:16793063 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16793063 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16793063 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16793063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16793063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16793063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16793063 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16793063 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16793063 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:16793063 | pubmed:author | pubmed-author:NordlundPärP | lld:pubmed |
| pubmed-article:16793063 | pubmed:author | pubmed-author:JohnsonKennet... | lld:pubmed |
| pubmed-article:16793063 | pubmed:author | pubmed-author:DouthwaiteSte... | lld:pubmed |
| pubmed-article:16793063 | pubmed:author | pubmed-author:HallbergB... | lld:pubmed |
| pubmed-article:16793063 | pubmed:author | pubmed-author:ErlandsenHeid... | lld:pubmed |
| pubmed-article:16793063 | pubmed:author | pubmed-author:BeuscherAlber... | lld:pubmed |
| pubmed-article:16793063 | pubmed:author | pubmed-author:EricssonUlrik... | lld:pubmed |
| pubmed-article:16793063 | pubmed:author | pubmed-author:AndersenNiels... | lld:pubmed |
| pubmed-article:16793063 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16793063 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:16793063 | pubmed:volume | 360 | lld:pubmed |
| pubmed-article:16793063 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16793063 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16793063 | pubmed:pagination | 774-87 | lld:pubmed |
| pubmed-article:16793063 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16793063 | pubmed:meshHeading | pubmed-meshheading:16793063... | lld:pubmed |
| pubmed-article:16793063 | pubmed:meshHeading | pubmed-meshheading:16793063... | lld:pubmed |
| pubmed-article:16793063 | pubmed:meshHeading | pubmed-meshheading:16793063... | lld:pubmed |
| pubmed-article:16793063 | pubmed:meshHeading | pubmed-meshheading:16793063... | lld:pubmed |
| pubmed-article:16793063 | pubmed:meshHeading | pubmed-meshheading:16793063... | lld:pubmed |
| pubmed-article:16793063 | pubmed:meshHeading | pubmed-meshheading:16793063... | lld:pubmed |
| pubmed-article:16793063 | pubmed:meshHeading | pubmed-meshheading:16793063... | lld:pubmed |
| pubmed-article:16793063 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16793063 | pubmed:articleTitle | The structure of the RNA m5C methyltransferase YebU from Escherichia coli reveals a C-terminal RNA-recruiting PUA domain. | lld:pubmed |
| pubmed-article:16793063 | pubmed:affiliation | Department of Medical Biochemistry and Biophysics, Karolinska Institute, 17177 Stockholm, Sweden. | lld:pubmed |
| pubmed-article:16793063 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16793063 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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