8e34: Difference between revisions
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==CryoEM structures of bAE1 captured in multiple states== | |||
<StructureSection load='8e34' size='340' side='right'caption='[[8e34]], [[Resolution|resolution]] 6.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8e34]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8E34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E34 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8e34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e34 OCA], [https://pdbe.org/8e34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e34 RCSB], [https://www.ebi.ac.uk/pdbsum/8e34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e34 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9XSW5_BOVIN Q9XSW5_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:36517642</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8e34" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Anion exchange protein 3D structures|Anion exchange protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Abuladze N]] | |||
[[Category: Azimov R]] | |||
[[Category: Jiang JS]] | |||
[[Category: Kao L]] | |||
[[Category: Kurtz I]] | |||
[[Category: Muhammad-Khan GH]] | |||
[[Category: Newman D]] | |||
[[Category: Noskov SY]] | |||
[[Category: Pushkin A]] | |||
[[Category: Tieleman P]] | |||
[[Category: Tsirulnikov K]] | |||
[[Category: Wang WG]] | |||
[[Category: Zhekova HR]] | |||
[[Category: Zhou ZH]] | |||
Latest revision as of 08:24, 12 June 2024
CryoEM structures of bAE1 captured in multiple statesCryoEM structures of bAE1 captured in multiple states
Structural highlights
FunctionPublication Abstract from PubMedAnion 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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