Messenger RNA conformations in the ribosomal E site revealed by X-ray crystallography.
A comparison of messenger RNA in X-ray crystal structures of 70S ribosomal complexes in the initiation, post-initiation and elongation states of translation shows distinct conformational differences in the exit (E) codon. Here, we present structural evidence indicating that, after the initiation event, the E codon nucleotides relax and form a classical A-helical conformation. This conformation is similar to that of the P and A codons, and is favourable for establishing Watson-Crick interactions with the anticodon of E-site transfer RNA.
Jenner
Lasse
L
Institut de Génétique et de Biologie Moléculaire et Cellulaire, 1, rue Laurent Fries, Illkirch 67404, France.
Rees
Bernard
B
Yusupov
Marat
M
Yusupova
Gulnara
G
D000926:Anticodon; D001483:Base Sequence; D003062:Codon; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010442:Peptide Chain Initiation, Translational; D012333:RNA, Messenger / Q000737:chemistry*; D012270:Ribosomes / Q000737:chemistry*; D016963:Thermus thermophilus / Q000737:chemistry*
D000926:Anticodon; D003062:Codon; D012333:RNA, Messenger