{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Huang H"],"funding":["Key Technologies Research and Development Program","National Science Fund for Distinguished Young Scholars","National Natural Science Foundation of China"],"pagination":["e1012376"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11271967"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(7)"],"pubmed_abstract":["Antimicrobial resistance is an ongoing \"one health\" challenge of global concern. The acyl-ACP synthetase (termed AasS) of the zoonotic pathogen Vibrio harveyi recycles exogenous fatty acid (eFA), bypassing the requirement of type II fatty acid synthesis (FAS II), a druggable pathway. A growing body of bacterial AasS-type isoenzymes compromises the clinical efficacy of FAS II-directed antimicrobials, like cerulenin. Very recently, an acyl adenylate mimic, C10-AMS, was proposed as a lead compound against AasS activity. However, the underlying mechanism remains poorly understood. Here we present two high-resolution cryo-EM structures of AasS liganded with C10-AMS inhibitor (2.33 Å) and C10-AMP intermediate (2.19 Å) in addition to its apo form (2.53 Å). Apart from our measurements for C10-AMS'"],"journal":["PLoS pathogens"],"pubmed_title":["An inhibitory mechanism of AasS, an exogenous fatty acid scavenger: Implications for re-sensitization of FAS II antimicrobials."],"pmcid":["PMC11271967"],"funding_grant_id":["32141001 & 31830001","32125003","2023YFC2307100 & 2023YFC2300021"],"pubmed_authors":["Zhou C","Huang H","Zhang H","Zhang X","Feng Y","Huang M","Qu J","Lu T","Chang S","Cui T"],"additional_accession":[]},"is_claimable":false,"name":"An inhibitory mechanism of AasS, an exogenous fatty acid scavenger: Implications for re-sensitization of FAS II antimicrobials.","description":"Antimicrobial resistance is an ongoing \"one health\" challenge of global concern. The acyl-ACP synthetase (termed AasS) of the zoonotic pathogen Vibrio harveyi recycles exogenous fatty acid (eFA), bypassing the requirement of type II fatty acid synthesis (FAS II), a druggable pathway. A growing body of bacterial AasS-type isoenzymes compromises the clinical efficacy of FAS II-directed antimicrobials, like cerulenin. Very recently, an acyl adenylate mimic, C10-AMS, was proposed as a lead compound against AasS activity. However, the underlying mechanism remains poorly understood. Here we present two high-resolution cryo-EM structures of AasS liganded with C10-AMS inhibitor (2.33 Å) and C10-AMP intermediate (2.19 Å) in addition to its apo form (2.53 Å). Apart from our measurements for C10-AMS'","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-02T05:04:29.675Z","creation":"2026-04-14T03:12:55.048Z"},"accession":"S-EPMC11271967","cross_references":{"pubmed":["39008531"],"doi":["10.1371/journal.ppat.1012376"]}}