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Entry
Database: PDB / ID: 8cte
TitleClass 2 of erythrocyte ankyrin-1 complex (Composite map)
Components
  • Ammonium transporter Rh type A
  • Ankyrin-1
  • Aquaporin-1
  • Band 3 anion transport protein
  • Blood group Rh(CE) polypeptide
  • Glycophorin-A
  • Protein 4.2
KeywordsTRANSPORT PROTEIN/STRUCTURAL PROTEIN / Membrane Protein / Anion Exchange / Erythrocyte / Glycoprotein / TRANSPORT PROTEIN-STRUCTURAL PROTEIN complex
Function / homology
Function and homology information


metanephric descending thin limb development / metanephric proximal straight tubule development / metanephric proximal convoluted tubule segment 2 development / metanephric glomerulus vasculature development / hydrogen peroxide channel activity / nitric oxide transmembrane transporter activity / lipid digestion / methylammonium transmembrane transport / Defective RHAG causes regulator type Rh-null hemolytic anemia (RHN) / Rhesus blood group biosynthesis ...metanephric descending thin limb development / metanephric proximal straight tubule development / metanephric proximal convoluted tubule segment 2 development / metanephric glomerulus vasculature development / hydrogen peroxide channel activity / nitric oxide transmembrane transporter activity / lipid digestion / methylammonium transmembrane transport / Defective RHAG causes regulator type Rh-null hemolytic anemia (RHN) / Rhesus blood group biosynthesis / methylammonium transmembrane transporter activity / Rhesus glycoproteins mediate ammonium transport / cellular response to salt stress / renal water transport / corticotropin secretion / carbon dioxide transmembrane transport / renal water absorption / carbon dioxide transmembrane transporter activity / glycerol transmembrane transporter activity / secretory granule organization / ammonium homeostasis / water transmembrane transporter activity / Passive transport by Aquaporins / cerebrospinal fluid secretion / positive regulation of saliva secretion / pancreatic juice secretion / establishment or maintenance of actin cytoskeleton polarity / spectrin-associated cytoskeleton / hemoglobin metabolic process / lateral ventricle development / positive regulation of organelle organization / glycerol transmembrane transport / cellular response to mercury ion / maintenance of epithelial cell apical/basal polarity / leak channel activity / protein-glutamine gamma-glutamyltransferase activity / intracellularly cGMP-activated cation channel activity / potassium ion transmembrane transporter activity / pH elevation / Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA) / intracellular water homeostasis / negative regulation of urine volume / NrCAM interactions / water transport / transepithelial water transport / Neurofascin interactions / water channel activity / Bicarbonate transporters / ammonium transmembrane transport / intracellular monoatomic ion homeostasis / ankyrin-1 complex / ammonium channel activity / glomerular filtration / CHL1 interactions / monoatomic anion transmembrane transporter activity / plasma membrane phospholipid scrambling / camera-type eye morphogenesis / cytoskeletal anchor activity / chloride:bicarbonate antiporter activity / fibroblast migration / multicellular organismal-level water homeostasis / solute:inorganic anion antiporter activity / cellular homeostasis / cellular hyperosmotic response / bicarbonate transport / bicarbonate transmembrane transporter activity / cell volume homeostasis / monoatomic anion transport / M band / hyperosmotic response / : / chloride transport / chloride transmembrane transporter activity / odontogenesis / positive regulation of fibroblast migration / Interaction between L1 and Ankyrins / ankyrin binding / : / nitric oxide transport / hemoglobin binding / spectrin binding / erythrocyte maturation / negative regulation of glycolytic process through fructose-6-phosphate / erythrocyte development / cortical cytoskeleton / exocytosis / brush border / axolemma / transmembrane transporter activity / cellular response to dexamethasone stimulus / potassium channel activity / endoplasmic reticulum to Golgi vesicle-mediated transport / renal water homeostasis / COPI-mediated anterograde transport / ephrin receptor binding / spleen development / cellular response to retinoic acid / protein-membrane adaptor activity / cytoskeleton organization / sensory perception of pain
Similarity search - Function
Aquaporin 1 / Blood group Rhesus C/E/D polypeptide / Glycophorin, conserved site / : / Glycophorin A / Glycophorin A signature. / Glycophorin / Mannitol-specific EII; Chain A / Mannitol-specific EII; Chain A / Coagulation Factor XIII; Chain A, domain 2 ...Aquaporin 1 / Blood group Rhesus C/E/D polypeptide / Glycophorin, conserved site / : / Glycophorin A / Glycophorin A signature. / Glycophorin / Mannitol-specific EII; Chain A / Mannitol-specific EII; Chain A / Coagulation Factor XIII; Chain A, domain 2 / Transglutaminase-like / Ammonium transporter fold / Ammonium transporter AmtB like domains / Ankyrin, UPA domain / UPA domain / : / Ammonium transporter AmtB-like domain / Ammonium Transporter Family / Transglutaminase, N-terminal / Transglutaminase, C-terminal / Transglutaminase, active site / Protein-glutamine gamma-glutamyltransferase, animal / Transglutaminase, C-terminal domain superfamily / : / Transglutaminase family / Transglutaminase family, C-terminal ig like domain / Transglutaminases active site. / Aquaporin transporter / Domain present in ZO-1 and Unc5-like netrin receptors / ZU5 domain / ZU5 domain / ZU5 domain profile. / Transglutaminase-like superfamily / Transglutaminase/protease-like homologues / Transglutaminase-like / Anion exchange protein 1 / Ammonium/urea transporter / Major intrinsic protein, conserved site / MIP family signature. / Transglutaminase-like superfamily / 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 / Major intrinsic protein / Major intrinsic protein / Phosphotransferase/anion transporter / Bicarbonate transporter, eukaryotic / Bicarbonate transporter-like, transmembrane domain / HCO3- transporter integral membrane domain / Aquaporin-like / Ankyrin repeat / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / Death-like domain superfamily / Ankyrin repeat / Papain-like cysteine peptidase superfamily / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Immunoglobulin E-set / Immunoglobulin-like fold / Immunoglobulins / Alpha-Beta Complex / Immunoglobulin-like / Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
CHOLESTEROL / Chem-PIO / Glycophorin-A / Band 3 anion transport protein / Ankyrin-1 / Protein 4.2 / Blood group Rh(CE) polypeptide / Aquaporin-1 / Ammonium transporter Rh type A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsVallese, F. / Kim, K. / Yen, L.Y. / Johnston, J.D. / Noble, A.J. / Cali, T. / Clarke, O.B.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat Struct Mol Biol / Year: 2022
Title: Architecture of the human erythrocyte ankyrin-1 complex.
Authors: Francesca Vallese / Kookjoo Kim / Laura Y Yen / Jake D Johnston / Alex J Noble / Tito Calì / Oliver Biggs Clarke /
Abstract: The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association ...The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering.
History
DepositionMay 14, 2022Deposition site: RCSB / Processing site: RCSB
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ankyrin-1
W: Band 3 anion transport protein
X: Protein 4.2
K: Blood group Rh(CE) polypeptide
L: Ammonium transporter Rh type A
Q: Ammonium transporter Rh type A
N: Glycophorin-A
D: Glycophorin-A
P: Band 3 anion transport protein
T: Band 3 anion transport protein
S: Aquaporin-1
O: Aquaporin-1
R: Aquaporin-1
M: Aquaporin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)879,44030
Polymers871,17914
Non-polymers8,26116
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 6 types, 13 molecules AWPTKLQNDSORM

#1: Protein Ankyrin-1 / ANK-1 / Ankyrin-R / Erythrocyte ankyrin


Mass: 206522.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P16157
#2: Protein Band 3 anion transport protein / Anion exchange protein 1 / AE 1 / Anion exchanger 1 / Solute carrier family 4 member 1


Mass: 101883.859 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P02730
#4: Protein Blood group Rh(CE) polypeptide / Rh polypeptide 1 / RhPI / Rh30A / RhIXB / Rhesus C/E antigens


Mass: 45598.918 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P18577
#5: Protein Ammonium transporter Rh type A / Erythrocyte membrane glycoprotein Rh50 / Erythrocyte plasma membrane 50 kDa glycoprotein / Rh50A / ...Erythrocyte membrane glycoprotein Rh50 / Erythrocyte plasma membrane 50 kDa glycoprotein / Rh50A / Rhesus blood group family type A glycoprotein / Rh family type A glycoprotein / Rh type A glycoprotein / Rhesus blood group-associated ammonia channel / Rhesus blood group-associated glycoprotein


Mass: 44229.629 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q02094
#6: Protein Glycophorin-A / MN sialoglycoprotein / PAS-2 / Sialoglycoprotein alpha


Mass: 16348.433 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P02724
#7: Protein
Aquaporin-1 / AQP-1 / Aquaporin-CHIP / Urine water channel / Water channel protein for red blood cells and kidney ...AQP-1 / Aquaporin-CHIP / Urine water channel / Water channel protein for red blood cells and kidney proximal tubule


Mass: 28788.320 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P29972

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Antibody / Sugars , 2 types, 3 molecules X

#10: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Antibody Protein 4.2 / P4.2 / Erythrocyte membrane protein band 4.2 / Erythrocyte protein 4.2


Mass: 77096.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P16452

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Non-polymers , 3 types, 14 molecules

#8: Chemical
ChemComp-CLR / CHOLESTEROL


Mass: 386.654 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C27H46O
#9: Chemical ChemComp-AJP / Digitonin


Mass: 1229.312 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C56H92O29 / Comment: detergent*YM
#11: Chemical ChemComp-PIO / [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate / dioctanoyl l-alpha-phosphatidyl-d-myo-inositol 4,5-diphosphate


Mass: 746.566 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C25H49O19P3 / Feature type: SUBJECT OF INVESTIGATION

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Details

Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Class 1 of erythrocyte ankyrin complex (composite map)
Type: COMPLEX / Entity ID: #1-#7 / Source: NATURAL
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
Details: Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v ...Details: Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
SpecimenConc.: 8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Details: Ankyrin complex mixture purified from digitonin-solubilized erythrocyte ghost membranes
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K / Details: 4-6 seconds, wait time 30 seconds

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1500 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 2.5 sec. / Electron dose: 58 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 2 / Num. of real images: 14464 / Details: Two grids were imaged in a single session.
EM imaging opticsEnergyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV

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Processing

SoftwareName: PHENIX / Version: 1.20.1_4487: / Classification: refinement
EM software
IDNameCategory
2Leginonimage acquisition
8PHENIXmodel refinement
13cryoSPARC3D reconstruction
CTF correctionDetails: Patch CTF (cryoSPARC v3) followed by per particle defocus refinement and refinement of higher order aberrations (cryoSPARC v3)
Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 145465
Details: Composite reconstruction; local refinements aligned to global consensus refinement, provided in additional maps.
Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00239723
ELECTRON MICROSCOPYf_angle_d0.47354059
ELECTRON MICROSCOPYf_dihedral_angle_d11.23314094
ELECTRON MICROSCOPYf_chiral_restr0.0386408
ELECTRON MICROSCOPYf_plane_restr0.0046698

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