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http://purl.uniprot.org/citations/33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33741963http://www.w3.org/2000/01/rdf-schema#comment"Pharmacological inhibition of vacuolar-type H+-ATPase (V-ATPase) by its specific inhibitor can abrogate tumor metastasis, prevent autophagy, and reduce cellular signaling responses. Bafilomycin A1, a member of macrolide antibiotics and an autophagy inhibitor, serves as a specific and potent V-ATPases inhibitor. Although there are many V-ATPase structures reported, the molecular basis of specific inhibitors on V-ATPase remains unknown. Here, we report the cryo-EM structure of bafilomycin A1 bound intact bovine V-ATPase at an overall resolution of 3.6-Å. The structure reveals six bafilomycin A1 molecules bound to the c-ring. One bafilomycin A1 molecule engages with two c subunits and disrupts the interactions between the c-ring and subunit a, thereby preventing proton translocation. Structural and sequence analyses demonstrate that the bafilomycin A1-binding residues are conserved in yeast and mammalian species and the 7'-hydroxyl group of bafilomycin A1 acts as a unique feature recognized by subunit c."xsd:string
http://purl.uniprot.org/citations/33741963http://purl.org/dc/terms/identifier"doi:10.1038/s41467-021-22111-5"xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/author"Wang R."xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/author"Lee C.H."xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/author"Hassan A."xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/author"Xie X.S."xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/pages"1782"xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/title"Molecular basis of V-ATPase inhibition by bafilomycin A1."xsd:string
http://purl.uniprot.org/citations/33741963http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/33741963http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33741963
http://purl.uniprot.org/citations/33741963http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33741963
http://purl.uniprot.org/uniprot/#_P61420-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963
http://purl.uniprot.org/uniprot/#_Q0VCV6-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963
http://purl.uniprot.org/uniprot/#_P23956-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963
http://purl.uniprot.org/uniprot/#_P39942-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963
http://purl.uniprot.org/uniprot/#_Q2TA24-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963
http://purl.uniprot.org/uniprot/#_Q3ZC23-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963
http://purl.uniprot.org/uniprot/#_Q28029-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963
http://purl.uniprot.org/uniprot/#_Q2KIB5-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963
http://purl.uniprot.org/uniprot/#_O46563-mappedCitation-33741963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33741963