7UZQ

Local refinement of RhAG-RhCE-ANK1(AR1-5), from consensus refinement of all classes

Summary for 7UZQ

• Entry DOI: 10.2210/pdb7uzq/pdb
• EMDB information: 26874 26886 26916 26917 26918 26919 26940 26943 26944 26948 26949 26950 26951 26952 26953 26954 26955 26956 26958 26960 26965 26972 26973 26974 26975 26978 26979 26982 26988
• Descriptor: Blood group Rh(CE) polypeptide, Ammonium transporter Rh type A, Ankyrin-1, ... (6 entities in total)
• Functional Keywords: membrane protein, anion exchange, erythrocyte, glycoprotein, transport protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 159050.60

Authors

Vallese, F.,Kim, K.,Yen, L.Y.,Johnston, J.D.,Noble, A.J.,Cali, T.,Clarke, O.B. (deposition date: 2022-05-09, release date: 2022-07-20, Last modification date: 2024-02-14)

Primary citation

Vallese, F.,Kim, K.,Yen, L.Y.,Johnston, J.D.,Noble, A.J.,Cali, T.,Clarke, O.B.
Architecture of the human erythrocyte ankyrin-1 complex.
Nat.Struct.Mol.Biol., 29:706-718, 2022

PubMed 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.

PubMed: 35835865
DOI: 10.1038/s41594-022-00792-w

Experimental method

ELECTRON MICROSCOPY (2.17 Å)