3vmf

Archaeal protein

spinqualitylabelsall models 3vmf, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vmf is a 2 chain structure with sequence from Aeropyrum pernix k1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GTP, MG, SO4 Gene: tuf, APE_1844 (Aeropyrum pernix K1), prf1, APE_1988.1 (Aeropyrum pernix K1) Resources: FirstGlance, OCA, RCSB, PDBsum Function [EF1A_AERPE] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity). [RF1_AERPE] Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA (By similarity). Publication Abstract from PubMed 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 (aEF1alpha), 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.aEF1alpha 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 aEF1alpha recognizes aRF1 and aPelota, another aRF1-related protein and molecular evolution of the three functions of aEF1alpha. Structural basis for translation termination by archaeal RF1 and GTP-bound EF1alpha complex.,Kobayashi K, Saito K, Ishitani R, Ito K, Nureki O Nucleic Acids Res. 2012 Jul 5. PMID:22772989 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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