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TitleThe cyclic octapeptide antibiotic argyrin B inhibits translation by trapping EF-G on the ribosome during translocation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 119, Issue 19, Page e2114214119, Year 2022
Publish dateMay 10, 2022
AuthorsMaximiliane Wieland / Mikael Holm / Emily J Rundlet / Martino Morici / Timm O Koller / Tinashe P Maviza / Domen Pogorevc / Ilya A Osterman / Rolf Müller / Scott C Blanchard / Daniel N Wilson /
PubMed AbstractArgyrins 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:35500116 / PubMed Central
MethodsEM (single particle)
Resolution2.58 - 2.9 Å
Structure data

13058

7otc

EMDB-13058, PDB-7otc:
Cryo-EM structure of an Escherichia coli 70S ribosome in complex with elongation factor G and the antibiotic Argyrin B
Method: EM (single particle) / Resolution: 2.9 Å

26486

7ug7

EMDB-26486, PDB-7ug7:
70S ribosome complex in an intermediate state of translocation bound to EF-G(GDP) stalled by Argyrin B
Method: EM (single particle) / Resolution: 2.58 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-PUT:
1,4-DIAMINOBUTANE / Putrescine

ChemComp-SPD:
SPERMIDINE / Spermidine

ChemComp-ZN:
Unknown entry

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

ChemComp-1I7:
Argyrin B

ChemComp-FME:
N-FORMYLMETHIONINE / N-Formylmethionine

ChemComp-PHE:
PHENYLALANINE / Phenylalanine

Source
  • escherichia coli bl21(de3) (bacteria)
  • escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
  • actinoplanes sp. (bacteria)
KeywordsRIBOSOME / antibiotic / translation / Translocation / EF-G / Argyrin

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