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- EMDB-34292: The outward-facing structure of hAE2 in basic pH -

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Basic information

Entry
Database: EMDB / ID: EMD-34292
TitleThe outward-facing structure of hAE2 in basic pH
Map data
Sample
  • Complex: hAE2 with bicarbonate
    • Protein or peptide: Anion exchange protein 2
Keywordschloride and bicarbonate transporter human-AE2 / TRANSPORT PROTEIN
Function / homology
Function and homology information


negative regulation of CD8-positive, alpha-beta T cell differentiation / negative regulation of CD8-positive, alpha-beta T cell proliferation / positive regulation of enamel mineralization / Bicarbonate transporters / amelogenesis / monoatomic anion transmembrane transporter activity / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity / digestive tract development / bicarbonate transport ...negative regulation of CD8-positive, alpha-beta T cell differentiation / negative regulation of CD8-positive, alpha-beta T cell proliferation / positive regulation of enamel mineralization / Bicarbonate transporters / amelogenesis / monoatomic anion transmembrane transporter activity / chloride:bicarbonate antiporter activity / solute:inorganic anion antiporter activity / digestive tract development / bicarbonate transport / monoatomic anion transport / regulation of bone resorption / transmembrane transporter activity / osteoclast differentiation / regulation of actin cytoskeleton organization / regulation of intracellular pH / transmembrane transport / spermatogenesis / basolateral plasma membrane / apical plasma membrane / focal adhesion / enzyme binding / membrane / plasma membrane
Similarity search - Function
Anion exchange protein 2 / Anion exchange protein / Anion exchange, conserved site / Anion exchangers family signature 1. / Anion exchangers family signature 2. / Band 3 cytoplasmic domain / Band 3 cytoplasmic domain / Phosphotransferase/anion transporter / Bicarbonate transporter, eukaryotic / Bicarbonate transporter-like, transmembrane domain / HCO3- transporter integral membrane domain
Similarity search - Domain/homology
Anion exchange protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.09 Å
AuthorsZhang Q / Jian L / Yao D / Rao B / Hu K / Xia Y / Cao Y
Funding support China, 2 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2018YFC1004704 China
National Natural Science Foundation of China (NSFC)82072468 China
CitationJournal: Nat Commun / Year: 2023
Title: The structural basis of the pH-homeostasis mediated by the Cl/HCO exchanger, AE2.
Authors: Qing Zhang / Liyan Jian / Deqiang Yao / Bing Rao / Ying Xia / Kexin Hu / Shaobai Li / Yafeng Shen / Mi Cao / An Qin / Jie Zhao / Yu Cao /
Abstract: The cell maintains its intracellular pH in a narrow physiological range and disrupting the pH-homeostasis could cause dysfunctional metabolic states. Anion exchanger 2 (AE2) works at high cellular pH ...The cell maintains its intracellular pH in a narrow physiological range and disrupting the pH-homeostasis could cause dysfunctional metabolic states. Anion exchanger 2 (AE2) works at high cellular pH to catalyze the exchange between the intracellular HCO and extracellular Cl, thereby maintaining the pH-homeostasis. Here, we determine the cryo-EM structures of human AE2 in five major operating states and one transitional hybrid state. Among those states, the AE2 shows the inward-facing, outward-facing, and intermediate conformations, as well as the substrate-binding pockets at two sides of the cell membrane. Furthermore, critical structural features were identified showing an interlock mechanism for interactions among the cytoplasmic N-terminal domain and the transmembrane domain and the self-inhibitory effect of the C-terminal loop. The structural and cell-based functional assay collectively demonstrate the dynamic process of the anion exchange across membranes and provide the structural basis for the pH-sensitive pH-rebalancing activity of AE2.
History
DepositionSep 15, 2022-
Header (metadata) releaseApr 12, 2023-
Map releaseApr 12, 2023-
UpdateJun 19, 2024-
Current statusJun 19, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_34292.png

Downloads & links

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Map

FileDownload / File: emd_34292.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 256 pix.
= 281.6 Å		1.1 Å/pix.
x 256 pix.
= 281.6 Å		1.1 Å/pix.
x 256 pix.
= 281.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.8
Minimum - Maximum-5.7492332 - 8.124347999999999
Average (Standard dev.)0.0023321377 (±0.14479086)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 281.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_34292_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_34292_half_map_2.map
Projections & Slices
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Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : hAE2 with bicarbonate

EntireName: hAE2 with bicarbonate
Components
  • Complex: hAE2 with bicarbonate
    • Protein or peptide: Anion exchange protein 2

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Supramolecule #1: hAE2 with bicarbonate

SupramoleculeName: hAE2 with bicarbonate / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 137 KDa

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Macromolecule #1: Anion exchange protein 2

MacromoleculeName: Anion exchange protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 137.176906 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSSAPRRPAK GADSFCTPEP ESLGPGTPGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE EPGRSYGEED FEYHRQSSHH IHHPLSTHL PPDARRRKTP QGPGRKPRRR PGASPTGETP TIEEGEEDED EASEAEGARA LTQPSPVSTP SSVQFFLQED D SADRKAER ...String:
MSSAPRRPAK GADSFCTPEP ESLGPGTPGF PEQEEDELHR TLGVERFEEI LQEAGSRGGE EPGRSYGEED FEYHRQSSHH IHHPLSTHL PPDARRRKTP QGPGRKPRRR PGASPTGETP TIEEGEEDED EASEAEGARA LTQPSPVSTP SSVQFFLQED D SADRKAER TSPSSPAPLP HQEATPRASK GAQAGTQVEE AEAEAVAVAS GTAGGDDGGA SGRPLPKAQP GHRSYNLQER RR IGSMTGA EQALLPRVPT DEIEAQTLAT ADLDLMKSHR FEDVPGVRRH LVRKNAKGST QSGREGREPG PTPRARPRAP HKP HEVFVE LNELLLDKNQ EPQWRETARW IKFEEDVEEE TERWGKPHVA SLSFRSLLEL RRTLAHGAVL LDLDQQTLPG VAHQ VVEQM VISDQIKAED RANVLRALLL KHSHPSDEKD FSFPRNISAG SLGSLLGHHH GQGAESDPHV TEPLMGGVPE TRLEV ERER ELPPPAPPAG ITRSKSKHEL KLLEKIPENA EATVVLVGCV EFLSRPTMAF VRLREAVELD AVLEVPVPVR FLFLLL GPS SANMDYHEIG RSISTLMSDK QFHEAAYLAD EREDLLTAIN AFLDCSVVLP PSEVQGEELL RSVAHFQRQM LKKREEQ GR LLPTGAGLEP KSAQDKALLQ MVEAAGAAED DPLRRTGRPF GGLIRDVRRR YPHYLSDFRD ALDPQCLAAV IFIYFAAL S PAITFGGLLG EKTQDLIGVS ELIMSTALQG VVFCLLGAQP LLVIGFSGPL LVFEEAFFSF CSSNHLEYLV GRVWIGFWL VFLALLMVAL EGSFLVRFVS RFTQEIFAFL ISLIFIYETF YKLVKIFQEH PLHGCSASNS SEVDGGENMT WAGARPTLGP GNRSLAGQS GQGKPRGQPN TALLSLVLMA GTFFIAFFLR KFKNSRFFPG RIRRVIGDFG VPIAILIMVL VDYSIEDTYT Q KLSVPSGF SVTAPEKRGW VINPLGEKSP FPVWMMVASL LPAILVFILI FMETQITTLI ISKKERMLQK GSGFHLDLLL IV AMGGICA LFGLPWLAAA TVRSVTHANA LTVMSKAVAP GDKPKIQEVK EQRVTGLLVA LLVGLSIVIG DLLRQIPLAV LFG IFLYMG VTSLNGIQFY ERLHLLLMPP KHHPDVTYVK KVRTLRMHLF TALQLLCLAL LWAVMSTAAS LAFPFILILT VPLR MVVLT RIFTDREMKC LDANEAEPVF DEREGVDEYN EMPMPV

UniProtKB: Anion exchange protein 2

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 26.0 µm / Nominal defocus min: 10.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.09 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 550035
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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