| pubmed-article:11744709 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C0337611 | lld:lifeskim |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C0028630 | lld:lifeskim |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C0018321 | lld:lifeskim |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C0030933 | lld:lifeskim |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C0178499 | lld:lifeskim |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:11744709 | lifeskim:mentions | umls-concept:C0086206 | lld:lifeskim |
| pubmed-article:11744709 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:11744709 | pubmed:dateCreated | 2002-2-18 | lld:pubmed |
| pubmed-article:11744709 | pubmed:abstractText | Nucleotide exchange in elongation factor Tu (EF-Tu) is catalyzed by elongation factor Ts (EF-Ts). Similarly to other GTP-binding proteins, the structural changes in the P loop and the Mg(2+) binding site are known to be important for nucleotide release from EF-Tu. In the present paper, we determine the contribution of the contacts between helix D of EF-Tu at the base side of the nucleotide and the N-terminal domain of EF-Ts to the catalysis. The rate constants of the multistep reaction between Escherichia coli EF-Tu, EF-Ts, and GDP were determined by stopped-flow kinetic analysis monitoring the fluorescence of either Trp-184 in EF-Tu or mant-GDP. Mutational analysis shows that contacts between helix D of EF-Tu and the N-terminal domain of EF-Ts are important for both complex formation and the acceleration of GDP dissociation. The kinetic results suggest that the initial contact of EF-Ts with helix D of EF-Tu weakens binding interactions around the guanine base, whereas contacts of EF-Ts with the phosphate binding side that promotes the release of the phosphate moiety of GDP appear to take place later. This "base-side-first" mechanism of guanine nucleotide release resembles that found for Ran x RCC1 and differs from mechanisms described for other GTPase x GEF complexes where interactions at the phosphate side of the nucleotide are released first. | lld:pubmed |
| pubmed-article:11744709 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11744709 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11744709 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11744709 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11744709 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11744709 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11744709 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11744709 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11744709 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11744709 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11744709 | pubmed:author | pubmed-author:WiedenHans-Jo... | lld:pubmed |
| pubmed-article:11744709 | pubmed:author | pubmed-author:RodninaMarina... | lld:pubmed |
| pubmed-article:11744709 | pubmed:author | pubmed-author:GromadskiKiri... | lld:pubmed |
| pubmed-article:11744709 | pubmed:author | pubmed-author:RodninDmytroD | lld:pubmed |
| pubmed-article:11744709 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11744709 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:11744709 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11744709 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11744709 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11744709 | pubmed:pagination | 6032-6 | lld:pubmed |
| pubmed-article:11744709 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:meshHeading | pubmed-meshheading:11744709... | lld:pubmed |
| pubmed-article:11744709 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11744709 | pubmed:articleTitle | Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base. | lld:pubmed |
| pubmed-article:11744709 | pubmed:affiliation | Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany. | lld:pubmed |
| pubmed-article:11744709 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11744709 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:944866 | entrezgene:pubmed | pubmed-article:11744709 | lld:entrezgene |
| entrez-gene:947838 | entrezgene:pubmed | pubmed-article:11744709 | lld:entrezgene |
| entrez-gene:948482 | entrezgene:pubmed | pubmed-article:11744709 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11744709 | lld:pubmed |
