Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-01399-2
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Funding
- Japan Society for the Promotion of Science (JSPS)
- Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT)
- ERATO Lipid Active Structure Project from Japan Science and Technology Agency (JST)
- Advanced Research for Medical Products Mining Programme of the National Institute of Biomedical Innovation (NIBIO) Japan
- Strategic International Cooperative Program (JST, Japan)
- Royal Society (UK)
- BBSRC (UK)
- International Human Frontier Science Program Organization (HFSPO)
- Herchel-Smith Scholarship
- MEXT
- Japan Agency for Medical Research and Development (AMED)
- BBSRC [BB/R00224X/1, BB/K017713/1] Funding Source: UKRI
- MRC [MC_PC_14116] Funding Source: UKRI
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The MacA-MacB-TolC tripartite complex is a transmembrane machine that spans both plasma membrane and outer membrane and actively extrudes substrates, including macrolide antibiotics, virulence factors, peptides and cell envelope precursors. These transport activities are driven by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. Here, we present the crystal structure of MacB at 3.4-angstrom resolution. MacB forms a dimer in which each protomer contains a nucleotide-binding domain and four transmembrane helices that protrude in the periplasm into a binding domain for interaction with the membrane fusion protein MacA. MacB represents an ABC transporter in pathogenic microorganisms with unique structural features.
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