8e34 | pdb_00008e34

CryoEM structures of bAE1 captured in multiple states

spinqualitylabelsall models 8e34, resolution 6.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8e34 is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9XSW5_BOVIN Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine.[ARBA:ARBA00002113] Publication Abstract from PubMed 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. CryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations.,Zhekova HR, Jiang J, Wang W, Tsirulnikov K, Kayik G, Khan HM, Azimov R, Abuladze N, Kao L, Newman D, Noskov SY, Tieleman DP, Hong Zhou Z, Pushkin A, Kurtz I Commun Biol. 2022 Dec 14;5(1):1372. doi: 10.1038/s42003-022-04306-8. PMID:36517642 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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