6GKI
Structure of E coli MlaC in Variously Loaded States
Summary for 6GKI
| Entry DOI | 10.2210/pdb6gki/pdb |
| Descriptor | Probable phospholipid-binding protein MlaC, BROMIDE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | lipid transfer outer membranes, lipid transport |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 2 |
| Total formula weight | 46548.79 |
| Authors | Knowles, T.J.,Lovering, A.L. (deposition date: 2018-05-21, release date: 2019-04-17, Last modification date: 2024-01-17) |
| Primary citation | Hughes, G.W.,Hall, S.C.L.,Laxton, C.S.,Sridhar, P.,Mahadi, A.H.,Hatton, C.,Piggot, T.J.,Wotherspoon, P.J.,Leney, A.C.,Ward, D.G.,Jamshad, M.,Spana, V.,Cadby, I.T.,Harding, C.,Isom, G.L.,Bryant, J.A.,Parr, R.J.,Yakub, Y.,Jeeves, M.,Huber, D.,Henderson, I.R.,Clifton, L.A.,Lovering, A.L.,Knowles, T.J. Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system. Nat Microbiol, 4:1692-1705, 2019 Cited by PubMed Abstract: The Mla pathway is believed to be involved in maintaining the asymmetrical Gram-negative outer membrane via retrograde phospholipid transport. The pathway is composed of three components: the outer membrane MlaA-OmpC/F complex, a soluble periplasmic protein, MlaC, and the inner membrane ATPase, MlaFEDB complex. Here, we solve the crystal structure of MlaC in its phospholipid-free closed apo conformation, revealing a pivoting β-sheet mechanism that functions to open and close the phospholipid-binding pocket. Using the apo form of MlaC, we provide evidence that the inner-membrane MlaFEDB machinery exports phospholipids to MlaC in the periplasm. Furthermore, we confirm that the phospholipid export process occurs through the MlaD component of the MlaFEDB complex and that this process is independent of ATP. Our data provide evidence of an apparatus for lipid export away from the inner membrane and suggest that the Mla pathway may have a role in anterograde phospholipid transport. PubMed: 31235958DOI: 10.1038/s41564-019-0481-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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