PMID- 29408956
OWN - NLM
STAT- MEDLINE
DCOM- 20190722
LR  - 20190722
IS  - 1362-4962 (Electronic)
IS  - 0305-1048 (Print)
IS  - 0305-1048 (Linking)
VI  - 46
IP  - 6
DP  - 2018 Apr 6
TI  - The structure of an elongation factor G-ribosome complex captured in the absence 
      of inhibitors.
PG  - 3211-3217
LID - 10.1093/nar/gky081 [doi]
AB  - During translation's elongation cycle, elongation factor G (EF-G) promotes 
      messenger and transfer RNA translocation through the ribosome. Until now, the 
      structures reported for EF-G-ribosome complexes have been obtained by trapping 
      EF-G in the ribosome. These results were based on use of non-hydrolyzable 
      guanosine 5'-triphosphate (GTP) analogs, specific inhibitors or a mutated EF-G 
      form. Here, we present the first cryo-electron microscopy structure of EF-G bound 
      to ribosome in the absence of an inhibitor. The structure reveals a natural 
      conformation of EF-G.GDP in the ribosome, with a previously unseen conformation 
      of its third domain. These data show how EF-G must affect translocation, and 
      suggest the molecular mechanism by which fusidic acid antibiotic prevents the 
      release of EF-G after GTP hydrolysis.
FAU - Mace, Kevin
AU  - Mace K
AD  - Univ. Rennes, CNRS, Institut de Genetique et de Developpement de Rennes (IGDR), 
      UMR6290, F35000 Rennes, France.
FAU - Giudice, Emmanuel
AU  - Giudice E
AD  - Univ. Rennes, CNRS, Institut de Genetique et de Developpement de Rennes (IGDR), 
      UMR6290, F35000 Rennes, France.
FAU - Chat, Sophie
AU  - Chat S
AD  - Univ. Rennes, CNRS, Institut de Genetique et de Developpement de Rennes (IGDR), 
      UMR6290, F35000 Rennes, France.
FAU - Gillet, Reynald
AU  - Gillet R
AD  - Univ. Rennes, CNRS, Institut de Genetique et de Developpement de Rennes (IGDR), 
      UMR6290, F35000 Rennes, France.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nucleic Acids Res
JT  - Nucleic acids research
JID - 0411011
RN  - 0 (Bacterial Proteins)
RN  - 0 (Peptide Elongation Factor G)
RN  - 0 (RNA, Messenger)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 9014-25-9 (RNA, Transfer)
SB  - IM
MH  - Bacterial Proteins/chemistry/*metabolism/ultrastructure
MH  - Cryoelectron Microscopy
MH  - Guanosine Triphosphate/metabolism
MH  - Hydrolysis
MH  - Models, Molecular
MH  - Molecular Conformation
MH  - Peptide Elongation Factor G/chemistry/*metabolism/ultrastructure
MH  - Protein Binding
MH  - *Protein Biosynthesis
MH  - Protein Conformation
MH  - RNA, Messenger/genetics/metabolism
MH  - RNA, Transfer/genetics/metabolism
MH  - Ribosomes/chemistry/*metabolism/ultrastructure
MH  - Thermus thermophilus/metabolism
PMC - PMC5887593
EDAT- 2018/02/07 06:00
MHDA- 2019/07/23 06:00
PMCR- 2018/02/02
CRDT- 2018/02/07 06:00
PHST- 2017/09/28 00:00 [received]
PHST- 2018/01/27 00:00 [accepted]
PHST- 2018/02/07 06:00 [pubmed]
PHST- 2019/07/23 06:00 [medline]
PHST- 2018/02/07 06:00 [entrez]
PHST- 2018/02/02 00:00 [pmc-release]
AID - 4835058 [pii]
AID - gky081 [pii]
AID - 10.1093/nar/gky081 [doi]
PST - ppublish
SO  - Nucleic Acids Res. 2018 Apr 6;46(6):3211-3217. doi: 10.1093/nar/gky081.