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TitleCryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations.
Journal, issue, pagesCommun Biol, Vol. 5, Issue 1, Page 1372, Year 2022
Publish dateDec 14, 2022
AuthorsHristina 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 /
PubMed AbstractAnion 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.
External linksCommun Biol / PubMed:36517642 / PubMed Central
MethodsEM (single particle)
Resolution4.4 - 6.3 Å
Structure data

EMDB-27267, PDB-8d9n:
CryoEM structures of bAE1 captured in multiple states.
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-27856, PDB-8e34:
CryoEM structures of bAE1 captured in multiple states
Method: EM (single particle) / Resolution: 6.0 Å

EMDB-28055, PDB-8eeq:
CryoEM structures of bAE1 captured in multiple states.
Method: EM (single particle) / Resolution: 6.3 Å

Source
  • bos taurus (cattle)
  • cattle (cattle)
KeywordsTRANSPORT PROTEIN / cryoEM / Band3 / bAE1 (SLC4A1) / anion exchanger / STRUCTURAL PROTEIN

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