| pubmed-article:17397188 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17397188 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:17397188 | lifeskim:mentions | umls-concept:C0018328 | lld:lifeskim |
| pubmed-article:17397188 | lifeskim:mentions | umls-concept:C0030933 | lld:lifeskim |
| pubmed-article:17397188 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:17397188 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:17397188 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:17397188 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
| pubmed-article:17397188 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:17397188 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:17397188 | pubmed:dateCreated | 2007-4-24 | lld:pubmed |
| pubmed-article:17397188 | pubmed:abstractText | Elongation factor Tu (EF-Tu) belongs to the family of GTP-binding proteins and requires elongation factor Ts (EF-Ts) for nucleotide exchange. Crystal structures suggested that one of the salient features in the EF-Tu x EF-Ts complex is a conformation change in the switch II region of EF-Tu that is initiated by intrusion of Phe81 of EF-Ts between His84 and His118 of EF-Tu and may result in a destabilization of Mg2+ coordination and guanine nucleotide release. In the present paper, the contribution of His84 to nucleotide release was studied by pre-steady-state kinetic analysis of nucleotide exchange in mutant EF-Tu in which His84 was replaced by Ala. Both intrinsic and EF-Ts-catalyzed nucleotide release was affected by the mutation, resulting in a 10-fold faster spontaneous GDP release and a 4-fold faster EF-Ts-catalyzed release of GTP and GDP. Removal of Mg2+ from the EF-Tu x EF-Ts complex increased the rate constant of GDP release 2-fold, suggesting a small contribution to nucleotide exchange. Together with published data on the effects of mutations interfering with other putative interactions between EF-Tu and EF-Ts, the results suggest that each of the contacts in the EF-Tu x EF-Ts complex alone contributes moderately to nucleotide destabilization, but together they act synergistically to bring about the overall 60,000-fold acceleration of nucleotide exchange in EF-Tu by EF-Ts. | lld:pubmed |
| pubmed-article:17397188 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17397188 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17397188 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17397188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17397188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17397188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17397188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17397188 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17397188 | pubmed:month | May | lld:pubmed |
| pubmed-article:17397188 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:17397188 | pubmed:author | pubmed-author:RodninaMarina... | lld:pubmed |
| pubmed-article:17397188 | pubmed:author | pubmed-author:GromadskiKiri... | lld:pubmed |
| pubmed-article:17397188 | pubmed:author | pubmed-author:SchümmerTobia... | lld:pubmed |
| pubmed-article:17397188 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17397188 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17397188 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:17397188 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17397188 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17397188 | pubmed:pagination | 4977-84 | lld:pubmed |
| pubmed-article:17397188 | pubmed:meshHeading | pubmed-meshheading:17397188... | lld:pubmed |
| pubmed-article:17397188 | pubmed:meshHeading | pubmed-meshheading:17397188... | lld:pubmed |
| pubmed-article:17397188 | pubmed:meshHeading | pubmed-meshheading:17397188... | lld:pubmed |
| pubmed-article:17397188 | pubmed:meshHeading | pubmed-meshheading:17397188... | lld:pubmed |
| pubmed-article:17397188 | pubmed:meshHeading | pubmed-meshheading:17397188... | lld:pubmed |
| pubmed-article:17397188 | pubmed:meshHeading | pubmed-meshheading:17397188... | lld:pubmed |
| pubmed-article:17397188 | pubmed:meshHeading | pubmed-meshheading:17397188... | lld:pubmed |
| pubmed-article:17397188 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17397188 | pubmed:articleTitle | Mechanism of EF-Ts-catalyzed guanine nucleotide exchange in EF-Tu: contribution of interactions mediated by helix B of EF-Tu. | lld:pubmed |
| pubmed-article:17397188 | pubmed:affiliation | Institute of Physical Biochemistry, University of Witten/Herdecke, D-58448 Witten, Germany. | lld:pubmed |
| pubmed-article:17397188 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17397188 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17397188 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17397188 | lld:pubmed |
