Source:http://linkedlifedata.com/resource/pubmed/id/10959626
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2000-11-29
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pubmed:abstractText |
The tertiary fold of the elongation factor, aEF-1beta, from Methanobacterium thermoautotrophicum was determined in a high-throughput fashion using a minimal set of NMR experiments. NMR secondary structure prediction, deuterium exchange experiments and the analysis of chemical shift perturbations were combined to identify the protein fold as an alpha-beta sandwich typical of many RNA binding proteins including EF-G. Following resolution of the tertiary fold, a high resolution structure of aEF-1beta was determined using heteronuclear and homonuclear NMR experiments and a semi-automated NOESY assignment strategy. Analysis of the aEF-1beta structure revealed close similarity to its human analogue, eEF-1beta. In agreement with studies on EF-Ts and human EF-1beta, a functional mechanism for nucleotide exchange is proposed wherein Phe46 on an exposed loop acts as a lever to eject GDP from the associated elongation factor G-protein, aEF-1alpha. aEF-1beta was also found to bind calcium in the groove between helix alpha2 and strand beta4. This novel feature was not observed previously and may serve a structural function related to protein stability or may play a functional role in archaeal protein translation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Archaeal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0925-2738
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
187-94
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10959626-Archaeal Proteins,
pubmed-meshheading:10959626-Calcium-Binding Proteins,
pubmed-meshheading:10959626-Humans,
pubmed-meshheading:10959626-Methanobacterium,
pubmed-meshheading:10959626-Models, Molecular,
pubmed-meshheading:10959626-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:10959626-Peptide Elongation Factor 1,
pubmed-meshheading:10959626-Protein Folding,
pubmed-meshheading:10959626-Protein Structure, Secondary,
pubmed-meshheading:10959626-Recombinant Fusion Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum.
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pubmed:affiliation |
McGill University, Department of Biochemistry, Montreal, PQ, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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