Progress on the Three-Dimensional Structural Determination of Trypsin-Modified EF-TU-GDP

  • Frances Jurnak
  • Michelle Nelson
  • Marilyn Yoder
  • Susan Heffron
  • Suet Miu

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.

Keywords

Beta Strand Elongation Cycle Ribose Ring Invariant Amino Acid Carboxy Terminal Region 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Frances Jurnak
    • 1
  • Michelle Nelson
    • 1
  • Marilyn Yoder
    • 1
  • Susan Heffron
    • 1
  • Suet Miu
    • 1
  1. 1.Department of BiochemistryUniversity of CaliforniaRiversideUSA

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