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摘要
En 中文
Translocation is an essential step of protein synthesis in which the large tRNA(2)-mRNA complex inside the ribosome moves from the A and P sites to the P and E sites, respectively, bringing a new mRNA codon into the decoding center. This process is catalyzed by the elongation factor EF-G-GTP (eEF2 in eukaryotes) and is the least understood stage of peptide elongation. Four new reports describe the crystal structures of translocation intermediates, illustrating important details of the translocation reaction.
Keyword:
CRYSTAL-STRUCTURE
MESSENGER-RNA
RIBOSOMAL TRANSLOCATION
GTP HYDROLYSIS
ACTIVATION
STATE
TU
MECHANISM
BINDING
SITE
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期刊
N
IF:
10.1
论文数:
4.8K
被引数:
2.8W
机构
引用论文
Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors
MOLECULAR CELL
IF16.6

