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Science. 2010 Nov 5;330(6005):835-838. doi: 10.1126/science.1194460.

The mechanism for activation of GTP hydrolysis on the ribosome.

Author information

1
MRC Laboratory of Molecular Biology, Cambridge, UK, CB2 0QH.
#
Contributed equally

Abstract

Protein synthesis requires several guanosine triphosphatase (GTPase) factors, including elongation factor Tu (EF-Tu), which delivers aminoacyl-transfer RNAs (tRNAs) to the ribosome. To understand how the ribosome triggers GTP hydrolysis in translational GTPases, we have determined the crystal structure of EF-Tu and aminoacyl-tRNA bound to the ribosome with a GTP analog, to 3.2 angstrom resolution. EF-Tu is in its active conformation, the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the γ-phosphate of GTP. This activated conformation is due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. The structure suggests a universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome.

PMID:
21051640
PMCID:
PMC3763471
DOI:
10.1126/science.1194460
[Indexed for MEDLINE]
Free PMC Article
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