Progress on the Three-Dimensional Structural Determination of Trypsin-Modified EF-TU-GDP
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.
KeywordsBeta Strand Elongation Cycle Ribose Ring Invariant Amino Acid Carboxy Terminal Region
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