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Open data
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Basic information
Entry | Database: PDB / ID: 8eeq | |||||||||
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Title | CryoEM structures of bAE1 captured in multiple states. | |||||||||
![]() | Anion exchange protein | |||||||||
![]() | TRANSPORT PROTEIN / cryoEM / Band3 / bAE1 (SLC4A1) / anion exchanger / STRUCTURAL PROTEIN | |||||||||
Function / homology | ![]() monoatomic anion transmembrane transporter activity / solute:inorganic anion antiporter activity / bicarbonate transmembrane transporter activity / regulation of intracellular pH / basolateral plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.3 Å | |||||||||
![]() | Zhekova, H.R. / Wang, W.G. / Jiang, J.S. / Tsirulnikov, K. / Muhammad-Khan, G.H. / Azimov, R. / Abuladze, N. / Kao, L. / Newman, D. / Noskov, S.Y. ...Zhekova, H.R. / Wang, W.G. / Jiang, J.S. / Tsirulnikov, K. / Muhammad-Khan, G.H. / Azimov, R. / Abuladze, N. / Kao, L. / Newman, D. / Noskov, S.Y. / Tieleman, P. / Zhou, Z.H. / Pushkin, A. / Kurtz, I. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: CryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations. Authors: Hristina R Zhekova / Jiansen Jiang / Weiguang Wang / Kirill Tsirulnikov / Gülru Kayık / Hanif Muhammad Khan / Rustam Azimov / Natalia Abuladze / Liyo Kao / Debbie Newman / Sergei Yu Noskov ...Authors: Hristina R Zhekova / Jiansen Jiang / Weiguang Wang / Kirill Tsirulnikov / Gülru Kayık / Hanif Muhammad Khan / Rustam Azimov / Natalia Abuladze / Liyo Kao / Debbie Newman / Sergei Yu Noskov / D Peter Tieleman / Z Hong Zhou / Alexander Pushkin / Ira Kurtz / ![]() ![]() Abstract: Anion exchanger 1 (AE1, band 3) is a major membrane protein of red blood cells and plays a key role in acid-base homeostasis, urine acidification, red blood cell shape regulation, and removal of ...Anion exchanger 1 (AE1, band 3) is a major membrane protein of red blood cells and plays a key role in acid-base homeostasis, urine acidification, red blood cell shape regulation, and removal of carbon dioxide during respiration. Though structures of the transmembrane domain (TMD) of three SLC4 transporters, including AE1, have been resolved previously in their outward-facing (OF) state, no mammalian SLC4 structure has been reported in the inward-facing (IF) conformation. Here we present the cryoEM structures of full-length bovine AE1 with its TMD captured in both IF and OF conformations. Remarkably, both IF-IF homodimers and IF-OF heterodimers were detected. The IF structures feature downward movement in the core domain with significant unexpected elongation of TM11. Molecular modeling and structure guided mutagenesis confirmed the functional significance of residues involved in TM11 elongation. Our data provide direct evidence for an elevator-like mechanism of ion transport by an SLC4 family member. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 326 KB | Display | ![]() |
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PDB format | ![]() | 240.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 28055MC ![]() 8d9nC ![]() 8e34C M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 104474.258 Da / Num. of mol.: 4 / Source method: isolated from a natural source Details: Chain A and C are the TMD of bovine AE1. Chain B and D are the cytoplasmic domain of bovine AE1. Some loops are missing because of insufficient resolution. Source: (natural) ![]() ![]() |
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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: Full-length bovine band 3 anion transport protein. / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: NATURAL | ||||||||||||||||||||
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Molecular weight | Value: 0.104 MDa / Experimental value: NO | ||||||||||||||||||||
Source (natural) | Organism: ![]() ![]() | ||||||||||||||||||||
Buffer solution | pH: 7.5 | ||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 0.4 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
Vitrification | Cryogen name: NITROGEN / Humidity: 100 % |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: OTHER / Calibrated magnification: 36764 X / Nominal defocus max: 3200 nm / Nominal defocus min: 1400 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 12 sec. / Electron dose: 52 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
Image scans | Movie frames/image: 48 / Used frames/image: 1-48 |
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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 | Details: Estimated by CTFFIND4. / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 2635578 | |||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | |||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 6.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 90818 / Num. of class averages: 1 / Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | |||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
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