6XBD
Cryo-EM structure of MlaFEDB in nanodiscs with phospholipid substrates
Summary for 6XBD
| Entry DOI | 10.2210/pdb6xbd/pdb |
| EMDB information | 22116 |
| Descriptor | Phospholipid ABC transporter-binding protein MlaD, Phospholipid ABC transporter permease protein MlaE, Phospholipid transport system ATP-binding protein MlaF, ... (6 entities in total) |
| Functional Keywords | lipid transport, bacterial cell envelope, mla pathway, mce |
| Biological source | Escherichia coli DEC6A More |
| Total number of polymer chains | 14 |
| Total formula weight | 296368.94 |
| Authors | Coudray, N.,Isom, G.L.,MacRae, M.R.,Saiduddin, M.,Ekiert, D.C.,Bhabha, G. (deposition date: 2020-06-05, release date: 2020-07-01, Last modification date: 2024-03-06) |
| Primary citation | Coudray, N.,Isom, G.L.,MacRae, M.R.,Saiduddin, M.N.,Bhabha, G.,Ekiert, D.C. Structure of bacterial phospholipid transporter MlaFEDB with substrate bound. Elife, 9:-, 2020 Cited by PubMed Abstract: In double-membraned bacteria, phospholipid transport across the cell envelope is critical to maintain the outer membrane barrier, which plays a key role in virulence and antibiotic resistance. An MCE transport system called Mla has been implicated in phospholipid trafficking and outer membrane integrity, and includes an ABC transporter, MlaFEDB. The transmembrane subunit, MlaE, has minimal sequence similarity to other transporters, and the structure of the entire inner-membrane MlaFEDB complex remains unknown. Here, we report the cryo-EM structure of MlaFEDB at 3.05 Å resolution, revealing distant relationships to the LPS and MacAB transporters, as well as the eukaryotic ABCA/ABCG families. A continuous transport pathway extends from the MlaE substrate-binding site, through the channel of MlaD, and into the periplasm. Unexpectedly, two phospholipids are bound to MlaFEDB, suggesting that multiple lipid substrates may be transported each cycle. Our structure provides mechanistic insight into substrate recognition and transport by MlaFEDB. PubMed: 33236984DOI: 10.7554/eLife.62518 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.05 Å) |
Structure validation
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