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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1985-7-17
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pubmed:abstractText |
The interaction between EF-Tu X GTP and aminoacyl-tRNA is shown to be influenced by mutations at site 375 of this three-domain protein. Site 375 is located in domain II near the interface with domain I [(1984) EMBO J. 3, 113-120]. Replacement of the alanine at this site by a threonine or valine residue results in lower binding constants with Phe-tRNA and Tyr-tRNA, as was evaluated by the hydrolysis protection technique. The data are discussed in the light of what is known about the three-dimensional structure of the protein and its interaction sites with aminoacyl-tRNA.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
185
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-6
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:3888672-Amino Acid Sequence,
pubmed-meshheading:3888672-Escherichia coli,
pubmed-meshheading:3888672-Guanosine Triphosphate,
pubmed-meshheading:3888672-Hydrolysis,
pubmed-meshheading:3888672-Kinetics,
pubmed-meshheading:3888672-Mutation,
pubmed-meshheading:3888672-Peptide Elongation Factor Tu,
pubmed-meshheading:3888672-Peptide Elongation Factors,
pubmed-meshheading:3888672-RNA, Transfer, Amino Acyl,
pubmed-meshheading:3888672-Structure-Activity Relationship
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pubmed:year |
1985
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pubmed:articleTitle |
Mutant species of EF-Tu, altered at position 375, exhibit a reduced affinity for aminoacylated transfer-RNAs.
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pubmed:publicationType |
Journal Article
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