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8E34

CryoEM structures of bAE1 captured in multiple states

8E34 の概要
エントリーDOI10.2210/pdb8e34/pdb
EMDBエントリー27856
分子名称Anion exchange protein (1 entity in total)
機能のキーワードcryoem, band3, bae1 (slc4a1), anion exchanger, structural protein, transport protein
由来する生物種Bos taurus (cattle)
タンパク質・核酸の鎖数2
化学式量合計208948.52
構造登録者
主引用文献Zhekova, 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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (6 Å)
構造検証レポート
Validation report summary of 8e34
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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