{"doi":"10.1016/j.resmic.2019.09.004","title":"An integrated transport mechanism of the maltose ABC importer","abstract":null,"journal":"Research in Microbiology","year":2019,"id":624864,"datarank":0.6782682865573562,"base_score":4.5217885770490405,"endowment":4.5217885770490405,"self_citation_contribution":0.6782682865573562,"citation_network_contribution":0.0,"self_endowment_contribution":0.6782682865573562,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":91,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":808784,"name":"Alessandra Narducci","orcid":"0000-0003-0453-6681","position":1,"is_corresponding":false},{"id":1170249,"name":"Douglas A. Griffith","orcid":null,"position":2,"is_corresponding":false},{"id":589359,"name":"Thorben Cordes","orcid":"0000-0002-8598-5499","position":3,"is_corresponding":false},{"id":1615459,"name":"Cédric Orelle","orcid":null,"position":4,"is_corresponding":false},{"id":984997,"name":"Rebecca Mächtel","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"An integrated transport mechanism of the maltose ABC importer","abstract":"ATP-binding cassette (ABC) transporters use the energy of ATP hydrolysis to transport a large diversity of molecules actively across biological membranes. A combination of biochemical, biophysical, and structural studies has established the maltose transporter MalFGK2 as one of the best characterized proteins of the ABC family. MalF and MalG are the transmembrane domains, and two MalKs form a homodimer of nucleotide-binding domains. A periplasmic maltose-binding protein (MalE) delivers maltose and other maltodextrins to the transporter, and triggers its ATPase activity. Substrate import occurs in a unidirectional manner by ATP-driven conformational changes in MalK2 that allow alternating access of the substrate-binding site in MalF to each side of the membrane. In this review, we present an integrated molecular mechanism of the transport process considering all currently available information. Furthermore, we summarize remaining inconsistencies and outline possible future routes to decipher the full mechanistic details of transport by MalEFGK2 complex and that of related importer systems.","is_dataset_classified":null,"base_score":4.5217885770490405,"endowment":4.5217885770490405,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"31560984","pmcid":"PMC6906923","openalex_id":"https://openalex.org/W2976142053","authors":[],"funders":[{"funder_name":"Agence Nationale de la Recherche","grant_id":"ANR-17-CE11-0045-01","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"SFB863","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"GRK2062","title":null},{"funder_name":"European Research Council","grant_id":"638536 \\u2013 SM-IMPORT","title":null},{"funder_name":"European Research Council","grant_id":"638536","title":"Substrate import at work: single-molecule studies of ABC transporters"},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"unidentified","title":"unidentified"},{"funder_name":"French National Research Agency (ANR)","grant_id":"ANR-17-CE11-0045","title":"Mechanism of antimicrobial peptide resistance mediated by an ABC transporter coupled to a two-component regulatory system in Streptococcus pneumoniae"}],"total_grants":7,"fwci":4.5627,"citation_percentile":0.95996614,"influential_citations":0,"citation_trend":[{"year":2019,"count":1},{"year":2020,"count":16},{"year":2021,"count":22},{"year":2022,"count":11},{"year":2023,"count":16},{"year":2024,"count":9},{"year":2025,"count":13},{"year":2026,"count":3}],"oa_status":"hybrid","license":"cc-by-nc-nd","oa_locations":[{"url":"https://www.sciencedirect.com/science/article/pii/S0923250819300981/pdf","host_type":"journal"},{"url":"https://www.sciencedirect.com/science/article/pii/S0923250819300981/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0923250819300981?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0923250819300981?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.resmic.2019.09.004","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/31560984","host_type":"repository"},{"url":"https://hal.science/hal-02376190","host_type":"repository"},{"url":"https://epub.ub.uni-muenchen.de/77653/","host_type":"journal"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6906923","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC6906923","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1016/j.resmic.2019.09.004","host_type":""},{"url":"https://dx.doi.org/10.1016/j.resmic.2019.09.004","host_type":""}],"fields_of_study":["Drug Transport and Resistance Mechanisms","Trace Elements in Health","Amino Acid Enzymes and Metabolism","0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":["Adenosine Triphosphate","Binding Sites","Biological Transport","Cell Membrane","Escherichia coli","Maltose","Models, Molecular","Polysaccharides","Protein Conformation","ATP-Binding Cassette Transporters","Escherichia coli Proteins","Periplasmic Binding Proteins"],"keywords":["Periplasmic space","ATP-binding cassette transporter","Maltose","Biology","ATP hydrolysis","Biochemistry","Transporter","Maltose-binding protein","ATPase","Cyclic nucleotide-binding domain","Walker motifs","Binding site","Transmembrane domain","Transmembrane protein","Nucleotide","Membrane","Enzyme","Gene","Receptor","Escherichia coli","ABC transporter","Epr Spectroscopy","Single Molecule Fluorescence","Importer","Smfret","Substrate-binding Protein","Models, Molecular","Binding Sites","Protein Conformation","Escherichia coli Proteins","Cell Membrane","Biological Transport","Article","Adenosine Triphosphate","Polysaccharides","Periplasmic Binding Proteins","ATP-Binding Cassette Transporters"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Affordable and clean energy"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"},{"name":"doi"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-04T05:05:43.135287Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}