期刊
SCIENCE
卷 330, 期 6005, 页码 835-838出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1194460
关键词
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资金
- Medical Research Council UK
- Wellcome Trust
- Agouron Institute
- Louis-Jeantet Foundation
- Gates-Cambridge scholarship
- MRC [MC_U105184332] Funding Source: UKRI
- Medical Research Council [MC_U105184332] Funding Source: researchfish
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 gamma-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.
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