Abstract:
:Recent collection of high-resolution crystal structures of the 70S ribosome with mRNA and tRNA substrates enhances our knowledge of protein synthesis principles. A novel network of interactions between the ribosome in the elongation state and mRNA downstream from the A codon suggests that mRNA is stabilized and aligned at the entrance to the decoding center. The X-ray studies clarify how natural modifications of tRNA are involved in the stabilization of the codon-anticodon interactions, prevention of frame-shifting and also expansion of the decoding capacity of tRNAs. In addition, the crystal structures provide the view that tRNA in the A and P sites communicate through a protein rich environment and suggest how these tRNAs are controlled through the intersubunit bridge formed by protein L31.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Demeshkina N,Jenner L,Yusupova G,Yusupov Mdoi
10.1016/j.sbi.2010.03.002subject
Has Abstractpub_date
2010-06-01 00:00:00pages
325-32issue
3eissn
0959-440Xissn
1879-033Xpii
S0959-440X(10)00040-0journal_volume
20pub_type
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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journal_title:Current opinion in structural biology
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