Abstract
Elongation factor (EF-)Tu is a cytoplasmic protein whose primary function is to recognize and transport aminoacyl tRNAs to the ribosome during protein synthesis (for review, see 1,2). In order to carry out its function, EF-Tu binds to different ligands, including GDP, GTP, EF-Ts, aminoacyl-tRNA and ribosomal proteins, during each elongation cycle. Biochemical studies have indicated that EF-Tu undergoes a series of discrete conformational changes as the protein changes ligands. The long-term objective of the crystallographic studies is to determine the atomic details of the conformational changes during the elongation cycle by X-ray diffraction techniques.
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Jurnak, F., Nelson, M., Yoder, M., Heffron, S., Miu, S. (1989). Progress on the Three-Dimensional Structural Determination of Trypsin-Modified EF-TU-GDP. In: Bosch, L., Kraal, B., Parmeggiani, A. (eds) The Guanine — Nucleotide Binding Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2037-2_2
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DOI: https://doi.org/10.1007/978-1-4757-2037-2_2
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