EMD-26949

Single-particle
2.5 Å
EMD-26949 Deposition: 10/05/2022
Map released: 20/07/2022
Last modified: 14/02/2024
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EMD-26949

Local refinement of RhAG/CE trimer, class 1 of erythrocyte ankyrin-1 complex

EMD-26949

Single-particle
2.5 Å
EMD-26949 Deposition: 10/05/2022
Map released: 20/07/2022
Last modified: 14/02/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: Erythrocyte ankyrin-1 complex
Fitted models: 7v0s (Avg. Q-score: 0.694)

Deposition Authors: Vallese F , Kim K , Yen LY, Johnston JD , Noble AJ , Cali T , Clarke OB
Architecture of the human erythrocyte ankyrin-1 complex.
Vallese F , Kim K , Yen LY, Johnston JD , Noble AJ , Cali T , Clarke OB
(2022) Nat Struct Mol Biol , 29 , 706 - 718
PUBMED: 35835865
DOI: doi:10.1038/s41594-022-00792-w
ISSN: 1545-9985
Abstract:
The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering.