7ug7

70S ribosome complex in an intermediate state of translocation bound to EF-G(GDP) stalled by Argyrin B

spinqualitylabelsall models 7ug7, resolution 2.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ug7 is a 10 chain structure with sequence from Actinoplanes sp., Escherichia coli and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.58Å Ligands: 0UO, 1MG, 2MA, 2MG, 3AU, 3TD, 4D4, 4OC, 4SU, 5MC, 5MU, 6MZ, BB9, D2T, DAL, DBB, DHA, FME, G7M, GDP, H2U, MA6, MG, MIA, OMC, OMG, OMU, PHE, PSU, PUT, SAR, SPD, UR3, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL20_ECOLI One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.[HAMAP-Rule:MF_00382] Publication Abstract from PubMed Argyrins are a family of naturally produced octapeptides that display promising antimicrobial activity against Pseudomonas aeruginosa. Argyrin B (ArgB) has been shown to interact with an elongated form of the translation elongation factor G (EF-G), leading to the suggestion that argyrins inhibit protein synthesis by interfering with EF-G binding to the ribosome. Here, using a combination of cryo-electron microscopy (cryo-EM) and single-molecule fluorescence resonance energy transfer (smFRET), we demonstrate that rather than interfering with ribosome binding, ArgB rapidly and specifically binds EF-G on the ribosome to inhibit intermediate steps of the translocation mechanism. Our data support that ArgB inhibits conformational changes within EF-G after GTP hydrolysis required for translocation and factor dissociation, analogous to the mechanism of fusidic acid, a chemically distinct antibiotic that binds a different region of EF-G. These findings shed light on the mechanism of action of the argyrin-class antibiotics on protein synthesis as well as the nature and importance of rate-limiting, intramolecular conformational events within the EF-G-bound ribosome during late-steps of translocation. The cyclic octapeptide antibiotic argyrin B inhibits translation by trapping EF-G on the ribosome during translocation.,Wieland M, Holm M, Rundlet EJ, Morici M, Koller TO, Maviza TP, Pogorevc D, Osterman IA, Muller R, Blanchard SC, Wilson DN Proc Natl Acad Sci U S A. 2022 May 10;119(19):e2114214119. doi: , 10.1073/pnas.2114214119. Epub 2022 May 2. PMID:35500116 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures Ribosome 3D structures

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