{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Perez Carrillo VH"],"funding":["Bundesministerium für Bildung und Forschung","DAAD-CONACYT","Deutsche Forschungsgemeinschaft","Friedrich-Schiller-Universität Jena","PROCOPE Mobility Fellowship","Hans Böckler Stiftung"],"pagination":["81-86"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9068644"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["ATP binding cassette (ABC) proteins are present in all phyla of life and form one of the largest protein families. The Bacillus subtilis ABC transporter BmrA is a functional homodimer that can extrude many different harmful compounds out of the cell. Each BmrA monomer is composed of a transmembrane domain (TMD) and a nucleotide binding domain (NBD). While the TMDs of ABC transporters are sequentially diverse, the highly conserved NBDs harbor distinctive conserved motifs that enable nucleotide binding and hydrolysis, interdomain communication and that mark a protein as a member of the ABC superfamily. In the catalytic cycle of an ABC transporter, the NBDs function as the molecular motor that fuels substrate translocation across the membrane via the TMDs and are thus pivotal for the entire t"],"journal":["Biomolecular NMR assignments"],"pubmed_title":["Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state."],"pmcid":["PMC9068644"],"funding_grant_id":["EXC 2051 – Project ID 390713860","Fulbright-Cottrell Award","HE7351/3-1"],"pubmed_authors":["Tran MA","Wiedemann C","Rose-Sperling D","Perez Carrillo VH","Hellmich UA"],"additional_accession":[]},"is_claimable":false,"name":"Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state.","description":"ATP binding cassette (ABC) proteins are present in all phyla of life and form one of the largest protein families. The Bacillus subtilis ABC transporter BmrA is a functional homodimer that can extrude many different harmful compounds out of the cell. Each BmrA monomer is composed of a transmembrane domain (TMD) and a nucleotide binding domain (NBD). While the TMDs of ABC transporters are sequentially diverse, the highly conserved NBDs harbor distinctive conserved motifs that enable nucleotide binding and hydrolysis, interdomain communication and that mark a protein as a member of the ABC superfamily. In the catalytic cycle of an ABC transporter, the NBDs function as the molecular motor that fuels substrate translocation across the membrane via the TMDs and are thus pivotal for the entire t","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2025-04-18T12:10:38.64Z","creation":"2025-04-06T21:48:20.592Z"},"accession":"S-EPMC9068644","cross_references":{"pubmed":["34988902"],"doi":["10.1007/s12104-021-10063-2"]}}