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8EEQ

CryoEM structures of bAE1 captured in multiple states.

Summary for 8EEQ
Entry DOI10.2210/pdb8eeq/pdb
EMDB information27267 27856 28055
DescriptorAnion exchange protein (1 entity in total)
Functional Keywordscryoem, band3, bae1 (slc4a1), anion exchanger, structural protein, transport protein
Biological sourceBos taurus (cattle)
Total number of polymer chains4
Total formula weight417897.03
Authors
Primary citationZhekova, H.R.,Jiang, J.,Wang, W.,Tsirulnikov, K.,Kayik, G.,Khan, H.M.,Azimov, R.,Abuladze, N.,Kao, L.,Newman, D.,Noskov, S.Y.,Tieleman, D.P.,Hong Zhou, Z.,Pushkin, A.,Kurtz, I.
CryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations.
Commun Biol, 5:1372-1372, 2022
Cited by
PubMed 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 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.
PubMed: 36517642
DOI: 10.1038/s42003-022-04306-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.3 Å)
Structure validation

238582

数据于2025-07-09公开中

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