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Fusidic acid resistance through changes in the dynamics of EF-G

ABSTRACT: HDX-MS was used to study the binding of FusB to EF-G

INSTRUMENT(S): Synapt MS

ORGANISM(S): Staphylococcus Aureus

SUBMITTER: Antonio Calabrese

LAB HEAD: Antonio Nickolas Calabrese

PROVIDER: PXD017491 | Pride | 2020-10-15

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	EFGC3_FusB.DnX	Other
	fbsaca_191217I_HDX_efg_02.raw.zip	Raw
	fbsaca_191217I_HDX_efg_03.raw.zip	Raw
	fbsaca_191217I_HDX_efg_05.raw.zip	Raw
	fbsaca_191217I_HDX_efg_07.raw.zip	Raw

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1 - 5 of 37

Publications

Fusidic acid resistance through changes in the dynamics of the drug target.

Tomlinson Jennifer H JH Kalverda Arnout P AP Calabrese Antonio N AN

Proceedings of the National Academy of Sciences of the United States of America 20200930 41

Antibiotic resistance in clinically important bacteria can be mediated by target protection mechanisms, whereby a protein binds to the drug target and protects it from the inhibitory effects of the antibiotic. The most prevalent source of clinical resistance to the antibiotic fusidic acid (FA) is expression of the FusB family of proteins that bind to the drug target (Elongation factor G [EF-G]) and promote dissociation of EF-G from FA-stalled ribosome complexes. FusB binding causes changes in bo ...[more]

PMID: 32999060

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