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Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog
Abstract
The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-tRNA Phe ), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate (GTP) analog GDPNP was determined by x-ray crystallography at 2.7 angstrom resolution. The ternary complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome. The EF-Tu-GDPNP component binds to one side of the acceptor helix of Phe-tRNA Phe involving all three domains of EF-Tu. Binding sites for the phenylalanylated CCA end and the phosphorylated 5′ end are located at domain interfaces, whereas the T stem interacts with the surface of the β-barrel domain 3. The binding involves many conserved residues in EF-Tu. The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus.
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Citations
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The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
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Metadata
- Authors
- Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B. F. C., & Nyborg, J.
- Venue
- Science
- Published
- 1995-12
- Volume
- 270
- Issue
- 5241
- Pages
- 1464-1472
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2000064612
- Cited by
- 851
- References
- 1
- FWCI
- 17.05
- Type
- journal article
- Language
- en
- Open access
- closed
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- Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B. F. C., & Nyborg, J. (1995). Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog. Science. https://doi.org/10.1126/science.270.5241.1464
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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