7LH3
Structure of human prestin in the presence of sodium sulfate
Summary for 7LH3
Entry DOI | 10.2210/pdb7lh3/pdb |
EMDB information | 23335 |
Descriptor | Prestin (1 entity in total) |
Functional Keywords | transporter family, membrane protein, lipid interaction, high resolution |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 164128.42 |
Authors | Ge, J.,Gouaux, E. (deposition date: 2021-01-21, release date: 2021-08-25, Last modification date: 2025-06-04) |
Primary citation | Ge, J.,Elferich, J.,Dehghani-Ghahnaviyeh, S.,Zhao, Z.,Meadows, M.,von Gersdorff, H.,Tajkhorshid, E.,Gouaux, E. Molecular mechanism of prestin electromotive signal amplification. Cell, 184:4669-, 2021 Cited by PubMed Abstract: Hearing involves two fundamental processes: mechano-electrical transduction and signal amplification. Despite decades of studies, the molecular bases for both remain elusive. Here, we show how prestin, the electromotive molecule of outer hair cells (OHCs) that senses both voltage and membrane tension, mediates signal amplification by coupling conformational changes to alterations in membrane surface area. Cryoelectron microscopy (cryo-EM) structures of human prestin bound with chloride or salicylate at a common "anion site" adopt contracted or expanded states, respectively. Prestin is ensconced within a perimeter of well-ordered lipids, through which it induces dramatic deformation in the membrane and couples protein conformational changes to the bulk membrane. Together with computational studies, we illustrate how the anion site is allosterically coupled to changes in the transmembrane domain cross-sectional area and the surrounding membrane. These studies provide insight into OHC electromotility by providing a structure-based mechanism of the membrane motor prestin. PubMed: 34390643DOI: 10.1016/j.cell.2021.07.034 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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