Domain motions of EF-G bound to the 70S ribosome: Insights from a hand-shaking between multi-resolution structures

Biophysical Journal

Volumn 79, Issue 3, 2000, Pages 1670-1678

  Wriggers, Willy ^a,b   Agrawal, Rajendra K ^c,e   Drew, Devin Lee ^a   McCammon, Andrew ^a   Frank, Joachim ^c,d  

^a San Diego   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c STATE UNIVERSITY OF NEW YORK   (United States)

^d HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^e WADSWORTH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; GUANOSINE DIPHOSPHATE;

ARTICLE; COMPUTER PROGRAM; CONFORMATIONAL TRANSITION; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; DENSITY; INFORMATION PROCESSING; METHODOLOGY; MOLECULAR MODEL; NONHUMAN; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; RIBOSOME SUBUNIT;

EID: 0033863336     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76416-2     Document Type: Article

References (14)

1. Ævarsson, A. 1995. Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation. J. Mol. Evol. 41:1096-1104.
2. Ævarsson, A., E. Brazhnikov, M. Garber, J. Zheltonosova, Y. Chirgadze, S. al-Karadaghi, L. A. Svensson, and A. Liljas. 1994. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J. 13:3669-3677.
3. Agrawal, R. K., A. B. Heagle, and J. Frank. 2000. Studies of elongation factor G-dependent tRNA translocation by three-dimensional cryoelectron microscopy. In The Ribosome: Structure, Function, Antibiotics, and Cellular Interaction. R. A. Garrett, S. R. Donthwaite, A. Liljas, A. T. Matheson, P. B. Moore, and H. F. Noller, editors. ASM Press, Washington, DC. 53-62.
4. Agrawal, R. K., A. B. Heagle, P. Penczek, R. A. Grassucci, and J. Frank. 1999. EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nat. Struct. Biol. 6:643-647.
5. Agrawal, R. K., P. Penczek, R. A. Grassucci, and J. Frank. 1998. Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation. Proc. Natl. Acad. Sci. USA. 95:6134-6138.
6. Alberts, B. 1998. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell. 92:291-294.
7. Baca, O. G., M. S. Rohrbach, and J. W. Bodley. 1976. Equilibrium measurements of the interactions of guanine nucleotides with Escherichia coli elongation factor G and the ribosome. Biochemistry. 15:4570-4574.
8. Ban, N., P. Nissen, J. Hansen, M. Capel, P. B. Moore, and T. A. Steitz. 1999. Placement of protein and RNA structures into a 5 Å-resolution map of the 50S ribosomal subunit. Nature. 400:841-847.
9. Berchtold, H., L. Reshetnikova, C. O. Reiser, N. K. Schirmer, M. Sprinzl, and R. Hilgenfeld. 1993. Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature. 365:126-132.
10. Bourne, H. R., D. A. Sanders, and F. McCormick. 1990. The GTPase superfamily: a conserved switch for diverse cell functions. Nature. 348:125-132.
11. Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 349:117-127.
12. Brooks, B., R. Bruccoleri, B. Olafson, D. States, S. Swaminathan, and M. Karplus. 1983. CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comp. Chem. 4:187-217.
13. Brünger, A. 1992. X-PLOR, Version 3.1: A System for X-ray Crystallography and NMR. The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University.
14. Cate, J. H., M. M. Yusupov, G. Z. Yusupova, T. N. Earnest, and H. F. Noller. 1999. X-ray crystal structures of 70S ribosome functional complexes. Science. 285:2095-2104.