The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold.
The refined crystal structure of the ternary complex of yeast Phe-tRNAPhe, Thermus aquaticus elongation factor EF-Tu and the non-hydrolyzable GTP analog, GDPNP, reveals many details of the EF-Tu recognition of aminoacylated tRNA (aa-tRNA). EF-Tu-GTP recognizes the aminoacyl bond and one side of the backbone fold of the acceptor helix and has a high affinity for all ordinary elongator aa-tRNAs by binding to this aa-tRNA motif. Yet, the binding of deacylated tRNA, initiator tRNA, and selenocysteine-specific tRNA (tRNASec) is effectively discriminated against. Subtle rearrangements of the binding pocket may occur to optimize the fit to any side chain of the aminoacyl group and interactions with EF-Tu stabilize the 3'-aminoacyl isomer of aa-tRNA. A general complementarity is observed in the location of the binding sites in tRNA for synthetases and for EF-Tu. The complex formation is highly specific for the GTP-bound conformation of EF-Tu, which can explain the effects of various mutants.
Nissen
P
P
Department of Molecular and Structural Biology, Aarhus University, Denmark.
Kjeldgaard
M
M
Thirup
S
S
Clark
B F
BF
Nyborg
J
J
D001224:Aspartic Acid; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006160:Guanosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D006165:Guanylyl Imidodiphosphate / Q000737:chemistry / Q000378:metabolism; D008961:Models, Structural; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D012360:RNA, Transfer, Phe / Q000737:chemistry* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D013824:Thermus / Q000378:metabolism
D012360:RNA, Transfer, Phe; D001224:Aspartic Acid; D006165:Guanylyl Imidodiphosphate; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu