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Open data
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Basic information
Entry | Database: PDB / ID: 7sun | ||||||
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Title | Atomic model of prestin from gerbil (Meriones unguiculatus) | ||||||
![]() | Prestin, Enhanced Yellow Fluorescent Protein chimera | ||||||
![]() | MEMBRANE PROTEIN / MOTOR PROTEIN / Prestin (Slc26a5) / cochlear amplification / NonLinear Capacitance | ||||||
Function / homology | ![]() secondary active sulfate transmembrane transporter activity / sensory perception of sound / regulation of cell shape / basolateral plasma membrane / membrane => GO:0016020 Similarity search - Function | ||||||
Biological species | ![]() synthetic construct (others) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | ||||||
![]() | Butan, C. / Santos-Sacchi, J. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Single particle cryo-EM structure of the outer hair cell motor protein prestin. Authors: Carmen Butan / Qiang Song / Jun-Ping Bai / Winston J T Tan / Dhasakumar Navaratnam / Joseph Santos-Sacchi / ![]() Abstract: The mammalian outer hair cell (OHC) protein prestin (Slc26a5) differs from other Slc26 family members due to its unique piezoelectric-like property that drives OHC electromotility, the putative ...The mammalian outer hair cell (OHC) protein prestin (Slc26a5) differs from other Slc26 family members due to its unique piezoelectric-like property that drives OHC electromotility, the putative mechanism for cochlear amplification. Here, we use cryo-electron microscopy to determine prestin's structure at 3.6 Å resolution. Prestin is structurally similar to the anion transporter Slc26a9. It is captured in an inward-open state which may reflect prestin's contracted state. Two well-separated transmembrane (TM) domains and two cytoplasmic sulfate transporter and anti-sigma factor antagonist (STAS) domains form a swapped dimer. The transmembrane domains consist of 14 transmembrane segments organized in two 7+7 inverted repeats, an architecture first observed in the bacterial symporter UraA. Mutation of prestin's chloride binding site removes salicylate competition with anions while retaining the prestin characteristic displacement currents (Nonlinear Capacitance), undermining the extrinsic voltage sensor hypothesis for prestin function. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 247.1 KB | Display | ![]() |
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PDB format | ![]() | 192.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 965.8 KB | Display | ![]() |
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Full document | ![]() | 977.3 KB | Display | |
Data in XML | ![]() | 43.2 KB | Display | |
Data in CIF | ![]() | 65.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 25442MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 111865.805 Da / Num. of mol.: 2 / Fragment: prestin + linker + eYFP Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SLC26A5, PRES, eYFP / Cell line (production host): HEK293 / Production host: ![]() |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Prestin dimer surrounded by a belt of detergent / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.4 / Details: 10 mM HEPES, 200 mM NaCl, 0.02% GDN, pH 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2150 nm / Nominal defocus min: 1150 nm |
Image recording | Electron dose: 54 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 111863 / Symmetry type: POINT | ||||||||||||||||||||||||||||
Atomic model building | PDB-ID: 6RTF Accession code: 6RTF / Source name: PDB / Type: experimental model | ||||||||||||||||||||||||||||
Refine LS restraints |
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