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• W304055075 abstract "Research Article1 January 1984free access Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure. F.J. Duisterwinkel F.J. Duisterwinkel Search for more papers by this author B. Kraal B. Kraal Search for more papers by this author J.M. De Graaf J.M. De Graaf Search for more papers by this author A. Talens A. Talens Search for more papers by this author L. Bosch L. Bosch Search for more papers by this author G.W. Swart G.W. Swart Search for more papers by this author A. Parmeggiani A. Parmeggiani Search for more papers by this author T.F. La Cour T.F. La Cour Search for more papers by this author J. Nyborg J. Nyborg Search for more papers by this author B.F. Clark B.F. Clark Search for more papers by this author F.J. Duisterwinkel F.J. Duisterwinkel Search for more papers by this author B. Kraal B. Kraal Search for more papers by this author J.M. De Graaf J.M. De Graaf Search for more papers by this author A. Talens A. Talens Search for more papers by this author L. Bosch L. Bosch Search for more papers by this author G.W. Swart G.W. Swart Search for more papers by this author A. Parmeggiani A. Parmeggiani Search for more papers by this author T.F. La Cour T.F. La Cour Search for more papers by this author J. Nyborg J. Nyborg Search for more papers by this author B.F. Clark B.F. Clark Search for more papers by this author Author Information F.J. Duisterwinkel, B. Kraal, J.M. De Graaf, A. Talens, L. Bosch, G.W. Swart, A. Parmeggiani, T.F. La Cour, J. Nyborg and B.F. Clark The EMBO Journal (1984)3:113-120https://doi.org/10.1002/j.1460-2075.1984.tb01770.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Specific alterations of the elongation factor Tu (EF-Tu) polypeptide chain have been identified in a number of mutant species of this elongation factor. In two species, Ala-375, located on domain II, was found by amino acid analysis to be replaced by Thr and Val, respectively. These replacements substantially lower the affinity of EF-Tu.GDP for the antibiotic kirromycin. Since kirromycin can be cross-linked to Lys-357, also located on domain II but structurally very far from Ala-375, these data suggest that the replacements alter the relative position of domains I and II. The Ala-375 replacements also lower the dissociation rates of the binary complexes EF-Tu.GTP and the binding constants for EF-Tu.GTP and Phe-tRNA. It is conceivable that these effects are also mediated by movements of domains I and II relative to each other. Replacement of Gly-222 by Asp has been found in another mutant by DNA sequence analysis of the cloned tufB gene, coding for this mutant EF-Tu. Gly-222 is part of a structural domain, characteristic for a variety of nucleotide binding enzymes. Its replacement by Asp does not abolish the ability of EF-Tu to sustain protein synthesis. It increases the dissociation rate of EF-Tu.GTP by approximately 30%. In the presence of kirromycin this mutant species of EF-Tu.GDP does not bind to the ribosome, in contrast to its wild-type counterpart. A possible explanation is now open for experimental verification. Previous ArticleNext Article Volume 3Issue 11 January 1984In this issue RelatedDetailsLoading ..." @default.
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• W304055075 title "Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure." @default.
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