The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

C12070     2-[3,12-dihydroxy-13- [(2R,3R,4S,5S,6R)-4...

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of C12070

  • This paper reports the generation of Escherichia coli mutants resistant to pulvomycin [1].
  • In this work, the crystal structure of Thermus thermophilus EF-Tu x pulvomycin in complex with the GTP analogue guanylyl imino diphosphate (GDPNP) at 1.4 A resolution reveals an antibiotic binding site extending from the domain 1-3 interface to domain 2, overlapping the domain 1-2-3 junction [2].

High impact information on C12070

  • Together with targeted mutagenesis of the tufA gene, conditions were found to overcome membrane impermeability, thereby allowing the selection of three mutants harbouring elongation factor (EF)-Tu Arg230-->Cys, Arg333-->Cys or Thr334-->Ala which confer pulvomycin resistance [1].
  • Pulvomycin-resistant mutants of E.coli elongation factor Tu [1].
  • Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA [3].
  • As shown by Millipore filtration, chromatographic analysis, and hydrolysis protection experiments, pulvomycin prevents interaction between aminoacyl-tRNA and EF-Tu.GTP to yield the ternary complex aminoacyl-tRNA.EF-Tu.GTP [3].
  • Kirromycin and pulvomycin, antibiotics that specifically bind to EF-Tu and inhibit its activity in peptide elongation, also strongly inhibit EF-Tu-mediated renaturation of denatured rhodanese to levels near those observed for spontaneous, unassisted refolding [4].

Chemical compound and disease context of C12070

  • The C. acidophila system is totally insensitive to the EF-Tu targeted antibiotics pulvomycin (at 40 degrees C) and kirromycin (at 47-72 degrees C) contrary to control systems derived from both mesophilic (Escherichia coli) and thermoacidophilic (Bacillus acidocaldarius) eubacteria [5].

Biological context of C12070

  • Evidence was obtained that the EF-Tu binding site for GE2270 A is also distinct from those for kirromycin, pulvomycin, and aa-tRNA, even though this antibiotic functionally interferes with all three of these ligands [6].
  • Pulvomycin markedly affects the equilibrium and kinetics of the EF-Tu-nucleotide interaction, particularly of the EF-Tu.GTP complex [7].
  • The amino acid sequence of EF-Tul of P. rosea not only exhibits an unusual Tyr160 substitution (comparable to those described for kirromycin-resistant EF-Tus), but also shows significant changes of conserved amino acids in domain 2 that may be responsible for GE2270A resistance (the latter do not resemble those leading to pulvomycin resistance) [8].

Anatomical context of C12070


Associations of C12070 with other chemical compounds

  • The property of pulvomycin to modify selectively the conformation(s) of EF-Tu is also supported by its effect on heat- and urea-dependent denaturation, and tryptic digestion of the protein [7].
  • In order to analyze the functions of arginine residues located in domain II, with respect to pulvomycin resistance and the interaction with aminoacyl-tRNA, we have investigated the effect of the substitutions of the highly conserved residues Arg230 and Arg233 by site-directed mutagenesis [9].
  • The sensitivity of elongation factor Tu (EF-Tu) from different species of bacteria to the EF-Tu-binding antibiotics efrotomycin, pulvomycin and MDL 62879 was tested by measuring the effect of these antibiotics on cell-free protein synthesis systems [10].

Gene context of C12070

  • Kirromycin locks EF-Tu in the open conformation in the presence of either GTP or GDP, whereas pulvomycin locks the factor in the closed conformation [4].
  • The effects of pulvomycin and EF-Ts can coexist and are simply additive, supporting the conclusion that these two ligands interact with different sites of EF-Tu [7].


  1. Pulvomycin-resistant mutants of E.coli elongation factor Tu. Zeef, L.A., Bosch, L., Anborgh, P.H., Cetin, R., Parmeggiani, A., Hilgenfeld, R. EMBO J. (1994) [Pubmed]
  2. Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu. Parmeggiani, A., Krab, I.M., Okamura, S., Nielsen, R.C., Nyborg, J., Nissen, P. Biochemistry (2006) [Pubmed]
  3. Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP, and aminoacyl-tRNA. Wolf, H., Assmann, D., Fischer, E. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  4. Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing. Kudlicki, W., Coffman, A., Kramer, G., Hardesty, B. J. Biol. Chem. (1997) [Pubmed]
  5. Archaebacterial elongation factor Tu insensitive to pulvomycin and kirromycin. Cammarano, P., Teichner, A., Chinali, G., Londei, P., de Rosa, M., Gambacorta, A., Nicolaus, B. FEBS Lett. (1982) [Pubmed]
  6. Probing the reactivity of the GTP- and GDP-bound conformations of elongation factor Tu in complex with the antibiotic GE2270 A. Anborgh, P.H., Parmeggiani, A. J. Biol. Chem. (1993) [Pubmed]
  7. Effects of the antibiotic pulvomycin on the elongation factor Tu-dependent reactions. Comparison with other antibiotics. Anborgh, P.H., Okamura, S., Parmeggiani, A. Biochemistry (2004) [Pubmed]
  8. Elongation factor Tu1 of the antibiotic GE2270A producer Planobispora rosea has an unexpected resistance profile against EF-Tu targeted antibiotics. Möhrle, V.G., Tieleman, L.N., Kraal, B. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  9. Substitution of Arg230 and Arg233 in Escherichia coli elongation factor Tu strongly enhances its pulvomycin resistance. Boon, K., Krab, I., Parmeggiani, A., Bosch, L., Kraal, B. Eur. J. Biochem. (1995) [Pubmed]
  10. Sensitivity of elongation factor Tu (EF-Tu) from different bacterial species to the antibiotics efrotomycin, pulvomycin and MDL 62879. Landini, P., Bandera, M., Soffientini, A., Goldstein, B.P. J. Gen. Microbiol. (1993) [Pubmed]
WikiGenes - Universities