Conformational changes of elongation factor G on the ribosome during tRNA translocation.
Conformational changes of elongation factor G on the ribosome during tRNA translocation.
复制标题
DOI:
10.1016/j.cell.2014.11.049
复制
发表时间:
2015-01-15
期刊:
影响因子:
64.5
通讯作者:
Steitz TA
中科院分区:
文献类型:
--
作者:
Lin J;Gagnon MG;Bulkley D;Steitz TA
The universally conserved GTPase elongation factor G (EF-G) catalyzes the translocation of transfer RNA (tRNA) and messenger RNA (mRNA) on the ribosome after peptide bond formation. Despite numerous studies suggesting that EF-G undergoes extensive conformational rearrangements during translocation, high resolution structures exist for essentially only one conformation of EF-G in complex with the ribosome. Here, we report four atomic resolution crystal structures of EF-G bound to the ribosome programmed in the pre- and post-translocational states and to the ribosome trapped by the antibiotic dityromycin. We observe a previously unseen conformation of EF-G in the pretranslocation complex, which is independently captured by dityromycin on the ribosome. Our structures provide insights into the conformational space that EF-G samples on the ribosome and reveal that tRNA translocation on the ribosome is facilitated by a structural transition of EF-G from a compact to an elongated conformation, which can be prevented by the antibiotic dityromycin.
登录
查看更多内容
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
11.4
作者:
Holtkamp, Wolf;Cunha, Carlos E.;Rodnina, Marina V.
通讯作者:
Rodnina, Marina V.
DOI:
10.1038/10695
发表时间:
1999-07-01
期刊:
NATURE STRUCTURAL BIOLOGY
影响因子:
--
作者:
Agrawal, RK;Heagle, AB;Frank, J
通讯作者:
Frank, J
影响因子:
11.4
作者:
CZWORKOWSKI, J;WANG, J;MOORE, PB
通讯作者:
MOORE, PB
DOI:
10.1126/science.1179709
发表时间:
2009-10-30
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Gao YG;Selmer M;Dunham CM;Weixlbaumer A;Kelley AC;Ramakrishnan V
通讯作者:
Ramakrishnan V