| pubmed-article:21135207 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21135207 | lifeskim:mentions | umls-concept:C0037473 | lld:lifeskim |
| pubmed-article:21135207 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:21135207 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:21135207 | lifeskim:mentions | umls-concept:C0065917 | lld:lifeskim |
| pubmed-article:21135207 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:21135207 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:21135207 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:21135207 | pubmed:issue | 51 | lld:pubmed |
| pubmed-article:21135207 | pubmed:dateCreated | 2010-12-23 | lld:pubmed |
| pubmed-article:21135207 | pubmed:abstractText | The melibiose carrier from Escherichia coli (MelB) couples the accumulation of the disaccharide melibiose to the downhill entry of H(+), Na(+), or Li(+). In this work, substrate-induced FTIR difference spectroscopy was used in combination with fluorescence spectroscopy to quantitatively compare the conformational properties of MelB mutants, implicated previously in sodium binding, with those of a fully functional Cys-less MelB permease. The results first suggest that Asp55 and Asp59 are essential ligands for Na(+) binding. Secondly, though Asp124 is not essential for Na(+) binding, this acidic residue may play a critical role, possibly by its interaction with the bound cation, in the full Na(+)-induced conformational changes required for efficient coupling between the ion- and sugar-binding sites; this residue may also be a sugar ligand. Thirdly, Asp19 does not participate in Na(+) binding but it is a melibiose ligand. The location of these residues in two independent threading models of MelB is consistent with their proposed role. | lld:pubmed |
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| pubmed-article:21135207 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21135207 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21135207 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21135207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:21135207 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21135207 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:21135207 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:21135207 | pubmed:author | pubmed-author:PadrósEsteveE | lld:pubmed |
| pubmed-article:21135207 | pubmed:author | pubmed-author:Lórenz-Fonfrí... | lld:pubmed |
| pubmed-article:21135207 | pubmed:author | pubmed-author:LeblancGérard... | lld:pubmed |
| pubmed-article:21135207 | pubmed:author | pubmed-author:LeónXavierX | lld:pubmed |
| pubmed-article:21135207 | pubmed:author | pubmed-author:GranellMeritx... | lld:pubmed |
| pubmed-article:21135207 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21135207 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:21135207 | pubmed:volume | 107 | lld:pubmed |
| pubmed-article:21135207 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21135207 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21135207 | pubmed:pagination | 22078-83 | lld:pubmed |
| pubmed-article:21135207 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
| pubmed-article:21135207 | pubmed:meshHeading | pubmed-meshheading:21135207... | lld:pubmed |
| pubmed-article:21135207 | pubmed:meshHeading | pubmed-meshheading:21135207... | lld:pubmed |
| pubmed-article:21135207 | pubmed:meshHeading | pubmed-meshheading:21135207... | lld:pubmed |
| pubmed-article:21135207 | pubmed:meshHeading | pubmed-meshheading:21135207... | lld:pubmed |
| pubmed-article:21135207 | pubmed:meshHeading | pubmed-meshheading:21135207... | lld:pubmed |
| pubmed-article:21135207 | pubmed:meshHeading | pubmed-meshheading:21135207... | lld:pubmed |
| pubmed-article:21135207 | pubmed:meshHeading | pubmed-meshheading:21135207... | lld:pubmed |
| pubmed-article:21135207 | pubmed:meshHeading | pubmed-meshheading:21135207... | lld:pubmed |
| pubmed-article:21135207 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:21135207 | pubmed:articleTitle | Structural insights into the activation mechanism of melibiose permease by sodium binding. | lld:pubmed |
| pubmed-article:21135207 | pubmed:affiliation | Unitat de Biofísica, Departament de Bioquímica i de Biologia Molecular, Facultat de Medicina, and Centre d'Estudis en Biofísica, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain. | lld:pubmed |
| pubmed-article:21135207 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21135207 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
