| Autor: |
M.G. Cuypers, Chitra Subramanian, Stephen W. White, Emad Tajkhorshid, Charles O. Rock, Jessica M. Gullett, Shashank Pant, Christy R. Grace |
| Rok vydání: |
2021 |
| Předmět: |
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| DOI: |
10.1101/2021.09.16.460654 |
| Popis: |
Fatty acid (FA) transfer proteins extract FA from membranes and sequester their ligand to facilitate its movement through the cytosol. While detailed views of soluble protein-FA complexes are available, how FA exchange occurs at the membrane has remained unknown. Staphylococcus aureus FakB1 is a prototypical bacterial FA transfer protein that binds palmitate within a narrow, buried tunnel. Here, we determine the conformational change from this closed state to an open state that engages the phospholipid bilayer. Upon membrane binding, a dynamic loop in FakB1 that covers the FA binding site disengages and folds into an amphipathic helix. This helix inserts below the phosphate plane of the bilayer to create a diffusion channel for the FA to exchange between the protein and the membrane. The structure of the bilayer-associated conformation of FakB1 has local similarities with mammalian FA binding proteins and provides a general conceptual framework for how these proteins interact with the membrane to promote lipid transfer. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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