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)
 
Gene Review

TTHA1695  -  elongation factor G

Thermus thermophilus HB8

 
 
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 TTHA1695

 

High impact information on TTHA1695

  • The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A [3].
  • Two hypersensitive and two resistant variants of elongation factor-G (EF-G) toward fusidic acid are studied in comparison with the wild type factor [4].
  • Two elongation factors (EF) EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome [5].
  • Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome [5].
  • The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A [6].
 

Chemical compound and disease context of TTHA1695

  • Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid [4].
 

Biological context of TTHA1695

  • These results also suggest conformational changes of the EF-G molecule in the course of its interaction with the ribosome that might be induced by GTP binding and hydrolysis [5].
  • Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site [6].
  • The selected RNAs do not bind to elongation factor G. The EF-Tu binding RNAs share a short consensus sequence, 5'-ACCGAAG-3', which was also found in the alpha-sarcin domain of T. thermophilus23S rRNA [7].
 

Associations of TTHA1695 with chemical compounds

  • A correlation between fusidic acid resistance of EF-G mutants and their affinity to GTP are revealed in this study, although their interactions with GDP are not changed [4].

References

  1. Nucleotide sequence of the Thermus thermophilus HB8 gene coding for elongation factor G. Yakhnin, A.V., Vorozheykina, D.P., Matvienko, N.I. Nucleic Acids Res. (1989) [Pubmed]
  2. Structural insights into fusidic acid resistance and sensitivity in EF-G. Hansson, S., Singh, R., Gudkov, A.T., Liljas, A., Logan, D.T. J. Mol. Biol. (2005) [Pubmed]
  3. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. AEvarsson, A., Brazhnikov, E., Garber, M., Zheltonosova, J., Chirgadze, Y., al-Karadaghi, S., Svensson, L.A., Liljas, A. EMBO J. (1994) [Pubmed]
  4. Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid. Martemyanov, K.A., Liljas, A., Yarunin, A.S., Gudkov, A.T. J. Biol. Chem. (2001) [Pubmed]
  5. Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome. Martemyanov, K.A., Gudkov, A.T. J. Biol. Chem. (2000) [Pubmed]
  6. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. Laurberg, M., Kristensen, O., Martemyanov, K., Gudkov, A.T., Nagaev, I., Hughes, D., Liljas, A. J. Mol. Biol. (2000) [Pubmed]
  7. In vitro selected RNA molecules that bind to elongation factor Tu. Hornung, V., Hofmann, H.P., Sprinzl, M. Biochemistry (1998) [Pubmed]
 
WikiGenes - Universities