3VMF

Archaeal protein

Summary for 3VMF

• Entry DOI: 10.2210/pdb3vmf/pdb
• Descriptor: Elongation factor 1-alpha, Peptide chain release factor subunit 1, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: translation termination, translation
• Biological source: Aeropyrum pernix; More
• Cellular location: Cytoplasm (By similarity): Q9YAV0; Cytoplasm (Potential): Q9YAF1
• Total number of polymer chains: 2
• Total formula weight: 91666.25

Authors

Kobayashi, K.,Saito, K.,Ishitani, R.,Ito, K.,Nureki, O. (deposition date: 2011-12-12, release date: 2012-07-25, Last modification date: 2023-11-08)

Primary citation

Kobayashi, K.,Saito, K.,Ishitani, R.,Ito, K.,Nureki, O.
Structural basis for translation termination by archaeal RF1 and GTP-bound EF1alpha complex
Nucleic Acids Res., 40:9319-9328, 2012

PubMed Abstract: When a stop codon appears at the ribosomal A site, the class I and II release factors (RFs) terminate translation. In eukaryotes and archaea, the class I and II RFs form a heterodimeric complex, and complete the overall translation termination process in a GTP-dependent manner. However, the structural mechanism of the translation termination by the class I and II RF complex remains unresolved. In archaea, archaeal elongation factor 1 alpha (aEF1α), a carrier GTPase for tRNA, acts as a class II RF by forming a heterodimeric complex with archaeal RF1 (aRF1). We report the crystal structure of the aRF1·aEF1α complex, the first active class I and II RF complex. This structure remarkably resembles the tRNA·EF-Tu complex, suggesting that aRF1 is efficiently delivered to the ribosomal A site, by mimicking tRNA. It provides insights into the mechanism that couples GTP hydrolysis by the class II RF to stop codon recognition and peptidyl-tRNA hydrolysis by the class I RF. We discuss the different mechanisms by which aEF1α recognizes aRF1 and aPelota, another aRF1-related protein and molecular evolution of the three functions of aEF1α.

PubMed: 22772989
DOI: 10.1093/nar/gks660

Experimental method

X-RAY DIFFRACTION (2.3 Å)