7LGU

Structure of human prestin in the presence of NaCl

Summary for 7LGU

• Entry DOI: 10.2210/pdb7lgu/pdb
• EMDB information: 23329
• Descriptor: Prestin, CHLORIDE ION, CHOLESTEROL, ... (10 entities in total)
• Functional Keywords: transporter family, membrane protein, lipid interaction
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 178876.30

Authors

Ge, J.,Gouaux, E. (deposition date: 2021-01-21, release date: 2021-08-25, Last modification date: 2025-05-21)

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

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: 34390643
DOI: 10.1016/j.cell.2021.07.034

Experimental method

ELECTRON MICROSCOPY (2.3 Å)