1EFT

THE CRYSTAL STRUCTURE OF ELONGATION FACTOR EF-TU FROM THERMUS AQUATICUS IN THE GTP CONFORMATION

Summary for 1EFT

• Entry DOI: 10.2210/pdb1eft/pdb
• Descriptor: ELONGATION FACTOR TU, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
• Functional Keywords: elongation factor
• Biological source: Thermus aquaticus
• Cellular location: Cytoplasm: Q01698
• Total number of polymer chains: 1
• Total formula weight: 45275.45

Authors

Kjeldgaard, M.,Nissen, P.,Thirup, S.,Nyborg, J. (deposition date: 1993-08-24, release date: 1994-08-31, Last modification date: 2024-02-07)

Primary citation

Kjeldgaard, M.,Nissen, P.,Thirup, S.,Nyborg, J.
The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
Structure, 1:35-50, 1993

PubMed Abstract: Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected.

PubMed: 8069622
DOI: 10.1016/0969-2126(93)90007-4

Experimental method

X-RAY DIFFRACTION (2.5 Å)