| pubmed-article:16081328 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C0004594 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C0030933 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C1149036 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C1521805 | lld:lifeskim |
| pubmed-article:16081328 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16081328 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16081328 | pubmed:dateCreated | 2005-8-29 | lld:pubmed |
| pubmed-article:16081328 | pubmed:abstractText | The effect of noncatalytic domains 2+3 on the intrinsic activity and thermostability of the EF-Tu GTPase center was evaluated in experiments with isolated domains 1 and six chimeric variants of mesophilic Escherichia coli (Ec) and thermophilic Bacillus stearothermophilus (Bst) EF-Tus. The isolated catalytic domains 1 of both EF-Tus displayed similar GTPase activities at their optimal temperatures. However, noncatalytic domains 2+3 of the EF-Tus influenced the GTPase activity of domains 1 differently, depending on the domain origin. Ecdomains 2+3 suppressed the GTPase activity of the Ecdomain 1, whereas those of BstEF-Tu stimulated the Bstdomain 1 GTPase. Domain 1 and domains 2+3 of both EF-Tus positively cooperated to heat-stabilize their GTPase centers to attain optimal activity at a temperature close to the optimal growth temperature of either organism. This can be explained by a stabilization effect of domains 2+3 on alpha-helical regions of the G-domain as revealed by CD spectroscopy. | lld:pubmed |
| pubmed-article:16081328 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16081328 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16081328 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16081328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16081328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16081328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16081328 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16081328 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16081328 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:16081328 | pubmed:author | pubmed-author:JonákJiríJ | lld:pubmed |
| pubmed-article:16081328 | pubmed:author | pubmed-author:SanderováHana... | lld:pubmed |
| pubmed-article:16081328 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16081328 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:16081328 | pubmed:volume | 1752 | lld:pubmed |
| pubmed-article:16081328 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16081328 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16081328 | pubmed:pagination | 11-7 | lld:pubmed |
| pubmed-article:16081328 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:meshHeading | pubmed-meshheading:16081328... | lld:pubmed |
| pubmed-article:16081328 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16081328 | pubmed:articleTitle | Opposite roles of domains 2+3 of Escherichia coli EF-Tu and Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity. | lld:pubmed |
| pubmed-article:16081328 | pubmed:affiliation | Department of Gene Expression, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, 166 37 Prague 6, Czech Republic. | lld:pubmed |
| pubmed-article:16081328 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16081328 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:16081328 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947838 | entrezgene:pubmed | pubmed-article:16081328 | lld:entrezgene |
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| entrez-gene:2855072 | entrezgene:pubmed | pubmed-article:16081328 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16081328 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16081328 | lld:entrezgene |
