5ot7

Elongation factor G-ribosome complex captures in the absence of inhibitors.

Loading... Status: waiting for Mol* initialization Structural highlights 5ot7 is a 10 chain structure with sequence from Escherichia coli and Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.8Å Ligands: GDP, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RS2_THET8 Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit.[HAMAP-Rule:MF_00291_B] Publication Abstract from PubMed 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. The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors.,Mace K, Giudice E, Chat S, Gillet R Nucleic Acids Res. 2018 Feb 2. pii: 4835058. doi: 10.1093/nar/gky081. PMID:29408956 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures Ribosomal protein THX 3D structures Ribosome 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA