A T Gudkov

Summary

Country: Russia

Publications

  1. ncbi request reprint The L7/L12 ribosomal domain of the ribosome: structural and functional studies
    A T Gudkov
    Institute of Protein Research, Russian Academy of Sciences, Moscow Region
    FEBS Lett 407:253-6. 1997
  2. ncbi request reprint Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domain
    K A Martemyanov
    Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia
    Biochemistry (Mosc) 63:1216-9. 1998
  3. ncbi request reprint Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation
    K A Martemyanov
    Institute of Protein Research, Russian Academy of Sciences, Pushchino
    FEBS Lett 452:155-9. 1999
  4. ncbi request reprint Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid
    K A Martemyanov
    Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia
    J Biol Chem 276:28774-8. 2001
  5. ncbi request reprint [Mutational analysis of the functional role of the loop region in the elongation factor G fourth domain in the ribosomal translocation]
    A V Kolesnikov
    Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia
    Mol Biol (Mosk) 37:719-25. 2003
  6. pmc Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
    V N Uversky
    Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Russia
    Protein Sci 5:1844-51. 1996
  7. ncbi request reprint Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropin
    K A Martemyanov
    Institute of Protein Research, 142292 Pushchino, Moscow Region, Russia
    Protein Expr Purif 21:456-61. 2001
  8. ncbi request reprint An intact conformation at the tip of elongation factor G domain IV is functionally important
    K A Martemyanov
    Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region
    FEBS Lett 434:205-8. 1998
  9. ncbi request reprint Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
    M Laurberg
    Department of Molecular Biophysics, Centre for Chemistry and Chemical Engineering, Lund University, Lund, SE 221 00, Sweden
    J Mol Biol 303:593-603. 2000
  10. ncbi request reprint Stoichiometry and properties of the complex between ribosomal proteins L7 and L10 in solution
    A T Gudkov
    FEBS Lett 93:215-8. 1978

Collaborators

  • A Liljas
  • A S Spirin
  • V N Uversky
  • K A Martemyanov
  • A A Kovtun
  • E V Bocharov
  • A V Kolesnikov
  • M Laurberg
  • A S Yarunin
  • A G Minchenko
  • A S Arseniev
  • V A Shirokov
  • O V Kurnasov
  • D Hughes
  • I Nagaev
  • K Martemyanov
  • O Kristensen
  • E V Budovskaya

Detail Information

Publications13

  1. ncbi request reprint The L7/L12 ribosomal domain of the ribosome: structural and functional studies
    A T Gudkov
    Institute of Protein Research, Russian Academy of Sciences, Moscow Region
    FEBS Lett 407:253-6. 1997
    ..These changes occur upon interaction of the ribosome with the elongation factors and depend on GTP hydrolysis in accordance with the functional states of the ribosome...
  2. ncbi request reprint Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domain
    K A Martemyanov
    Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia
    Biochemistry (Mosc) 63:1216-9. 1998
    ..coli. The mutated protein with an uncleavable GTP analog also has an increased affinity to the ribosomes...
  3. ncbi request reprint Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation
    K A Martemyanov
    Institute of Protein Research, Russian Academy of Sciences, Pushchino
    FEBS Lett 452:155-9. 1999
    ..These results suggest that domain IV might be directly involved in translocation and GTPase activity of the factor is not directly coupled with translocation...
  4. ncbi request reprint Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid
    K A Martemyanov
    Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia
    J Biol Chem 276:28774-8. 2001
    ..The results presented in this paper indicate that fusidic acid-sensitive mutant factors have a conformation favorable for GTP binding and subsequent interaction with the ribosomes...
  5. ncbi request reprint [Mutational analysis of the functional role of the loop region in the elongation factor G fourth domain in the ribosomal translocation]
    A V Kolesnikov
    Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia
    Mol Biol (Mosk) 37:719-25. 2003
    ..The structural and biochemical data on the 30S subunit and EF-G were analyzed to specify the position of EF-G relative to the 30S and 50S ribosomal subunits...
  6. pmc Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
    V N Uversky
    Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Russia
    Protein Sci 5:1844-51. 1996
    ..Interaction of permuted protein with ligands leads to the structural adjustment and formation of active protein molecules...
  7. ncbi request reprint Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropin
    K A Martemyanov
    Institute of Protein Research, 142292 Pushchino, Moscow Region, Russia
    Protein Expr Purif 21:456-61. 2001
    ..The synthesis of functionally active antibacterial polypeptide cecropin P1 (31 amino acid residues) has been demonstrated...
  8. ncbi request reprint An intact conformation at the tip of elongation factor G domain IV is functionally important
    K A Martemyanov
    Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region
    FEBS Lett 434:205-8. 1998
    ..It is concluded that the native conformation of the loop is important for the factor-promoted translocation in the ribosome. The functional importance of the entire EF-G domain IV is discussed...
  9. ncbi request reprint Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
    M Laurberg
    Department of Molecular Biophysics, Centre for Chemistry and Chemical Engineering, Lund University, Lund, SE 221 00, Sweden
    J Mol Biol 303:593-603. 2000
    ..Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations...
  10. ncbi request reprint Stoichiometry and properties of the complex between ribosomal proteins L7 and L10 in solution
    A T Gudkov
    FEBS Lett 93:215-8. 1978
  11. ncbi request reprint Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10
    E V Bocharov
    Shemyakin Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow
    FEBS Lett 423:347-50. 1998
    ..Conformational motions on a millisecond time scale are detected in the (L7)4L10 complex. The possible relevance of these motions to the biological function of L7/L12 is discussed...
  12. ncbi request reprint Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution
    E V Bocharov
    Shemyakin Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation
    FEBS Lett 379:291-4. 1996
    ..The conformation of the NTD, which is responsible for the formation of the L7/L12 dimer, is alpha-helical hairpin. the NTD dimer forms an antiparallel four-alpha-helix bundle...
  13. ncbi request reprint [Mutation analysis of functional role of amino acid residues in domain IV of elongation factor G]
    A A Kovtun
    Mol Biol (Mosk) 40:850-6. 2006
    ..These loops are located at the tip of domain IV and close to the decoding center of the 30S ribosomal subunit upon EF-G interaction with the ribosome. The functional role of EF-G and its domain IV in ribosomal translocation is discussed...