7QP9
Outward-facing apo-form of auxin transporter PIN8
Summary for 7QP9
| Entry DOI | 10.2210/pdb7qp9/pdb |
| Related | 7QPA 7QPC |
| EMDB information | 14115 14118 |
| Descriptor | Auxin efflux carrier component 8, 1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total) |
| Functional Keywords | auxin transport, aec family, bart superfamily, membrane protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 86210.41 |
| Authors | Ung, K.L.,Winkler, M.B.L.,Dedic, E.,Stokes, D.L.,Pedersen, B.P. (deposition date: 2022-01-03, release date: 2022-07-06, Last modification date: 2024-11-13) |
| Primary citation | Ung, K.L.,Winkler, M.,Schulz, L.,Kolb, M.,Janacek, D.P.,Dedic, E.,Stokes, D.L.,Hammes, U.Z.,Pedersen, B.P. Structures and mechanism of the plant PIN-FORMED auxin transporter. Nature, 609:605-610, 2022 Cited by PubMed Abstract: Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants. The proteins in the PIN-FORMED (PIN) family (also known as the auxin efflux carrier family) are key participants in this process and control auxin export from the cytosol to the extracellular space. Owing to a lack of structural and biochemical data, the molecular mechanism of PIN-mediated auxin transport is not understood. Here we present biophysical analysis together with three structures of Arabidopsis thaliana PIN8: two outward-facing conformations with and without auxin, and one inward-facing conformation bound to the herbicide naphthylphthalamic acid. The structure forms a homodimer, with each monomer divided into a transport and scaffold domain with a clearly defined auxin binding site. Next to the binding site, a proline-proline crossover is a pivot point for structural changes associated with transport, which we show to be independent of proton and ion gradients and probably driven by the negative charge of the auxin. The structures and biochemical data reveal an elevator-type transport mechanism reminiscent of bile acid/sodium symporters, bicarbonate/sodium symporters and sodium/proton antiporters. Our results provide a comprehensive molecular model for auxin recognition and transport by PINs, link and expand on a well-known conceptual framework for transport, and explain a central mechanism of polar auxin transport, a core feature of plant physiology, growth and development. PubMed: 35768502DOI: 10.1038/s41586-022-04883-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.89 Å) |
Structure validation
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