A T Gudkov
- The L7/L12 ribosomal domain of the ribosome: structural and functional studiesA 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...
- Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domainK 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...
- Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocationK 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...
- Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acidK 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...
- [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...
- Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligandsV 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...
- Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropinK 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...
- An intact conformation at the tip of elongation factor G domain IV is functionally importantK 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...
- Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding siteM 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...
- Stoichiometry and properties of the complex between ribosomal proteins L7 and L10 in solutionA T Gudkov
FEBS Lett 93:215-8. 1978
- Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10E 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...
- Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solutionE 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...
- [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...