Structural basis for mRNA and tRNA positioning on the ribosome.
Protein synthesis requires the accurate positioning of mRNA and tRNA in the peptidyl-tRNA site of the ribosome. Here we describe x-ray crystal structures of the intact bacterial ribosome from Escherichia coli in a complex with mRNA and the anticodon stem-loop of P-site tRNA. At 3.5-A resolution, these structures reveal rearrangements in the intact ribosome that clamp P-site tRNA and mRNA on the small ribosomal subunit. Binding of the anticodon stem-loop of P-site tRNA to the ribosome is sufficient to lock the head of the small ribosomal subunit in a single conformation, thereby preventing movement of mRNA and tRNA before mRNA decoding.
Berk
Veysel
V
Department of Molecular and Cell Biology, and Chemistry, University of California, Berkeley, CA 94720, USA.
Zhang
Wen
W
Pai
Raj D
RD
Cate
Jamie H D
JH
Cate
Jamie H Doudna
JH
D001483:Base Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012333:RNA, Messenger / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012343:RNA, Transfer / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000737:chemistry / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D012333:RNA, Messenger; D012269:Ribosomal Proteins; D012343:RNA, Transfer