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- PDB-7uzq: Local refinement of RhAG-RhCE-ANK1(AR1-5), from consensus refinem... -

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Basic information

Entry
Database: PDB / ID: 7uzq
TitleLocal refinement of RhAG-RhCE-ANK1(AR1-5), from consensus refinement of all classes
Components
  • Ammonium transporter Rh type A
  • Ankyrin-1
  • Blood group Rh(CE) polypeptide
KeywordsTRANSPORT PROTEIN / Membrane Protein / Anion Exchange / Erythrocyte / Glycoprotein
Function / homology
Function and homology information


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 / carbon dioxide transmembrane transport / carbon dioxide transmembrane transporter activity / ammonium homeostasis / spectrin-associated cytoskeleton / positive regulation of organelle organization ...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 / carbon dioxide transmembrane transport / carbon dioxide transmembrane transporter activity / ammonium homeostasis / spectrin-associated cytoskeleton / positive regulation of organelle organization / maintenance of epithelial cell apical/basal polarity / leak channel activity / NrCAM interactions / Neurofascin interactions / ammonium transmembrane transport / intracellular monoatomic ion homeostasis / ankyrin-1 complex / ammonium channel activity / CHL1 interactions / cytoskeletal anchor activity / bicarbonate transport / M band / : / Interaction between L1 and Ankyrins / ankyrin binding / spectrin binding / erythrocyte development / exocytosis / axolemma / endoplasmic reticulum to Golgi vesicle-mediated transport / COPI-mediated anterograde transport / cytoskeleton organization / sarcoplasmic reticulum / protein localization to plasma membrane / carbon dioxide transport / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / sarcolemma / structural constituent of cytoskeleton / multicellular organismal-level iron ion homeostasis / cytoplasmic side of plasma membrane / Z disc / ATPase binding / protein phosphatase binding / basolateral plasma membrane / transmembrane transporter binding / postsynaptic membrane / cytoskeleton / neuron projection / structural molecule activity / enzyme binding / signal transduction / membrane / plasma membrane / cytosol
Similarity search - Function
Blood group Rhesus C/E/D polypeptide / Ammonium transporter fold / Ammonium transporter AmtB like domains / Ankyrin, UPA domain / UPA domain / : / Ammonium transporter AmtB-like domain / Ammonium Transporter Family / Domain present in ZO-1 and Unc5-like netrin receptors / ZU5 domain ...Blood group Rhesus C/E/D polypeptide / Ammonium transporter fold / Ammonium transporter AmtB like domains / Ankyrin, UPA domain / UPA domain / : / Ammonium transporter AmtB-like domain / Ammonium Transporter Family / Domain present in ZO-1 and Unc5-like netrin receptors / ZU5 domain / ZU5 domain / ZU5 domain profile. / Ammonium/urea transporter / 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 / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
CHOLESTEROL / Ankyrin-1 / Blood group Rh(CE) polypeptide / Ammonium transporter Rh type A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.17 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 9, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 20, 2022Provider: repository / Type: Initial release
Revision 1.1Jul 27, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Feb 14, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_3d_fitting_list / pdbx_initial_refinement_model
Item: _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id ..._em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
K: Blood group Rh(CE) polypeptide
L: Ammonium transporter Rh type A
Q: Ammonium transporter Rh type A
J: Ankyrin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)159,0518
Polymers155,8194
Non-polymers3,2324
Water4,234235
1


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

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Components

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Protein , 3 types, 4 molecules KLQJ

#1: 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) / Organ: Blood / Tissue: Erythrocytes / References: UniProt: P18577
#2: 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) / Organ: Blood / Tissue: Erythrocytes / References: UniProt: Q02094
#3: Protein Ankyrin-1 / ANK-1 / Ankyrin-R / Erythrocyte ankyrin


Mass: 21760.494 Da / Num. of mol.: 1 / Fragment: AR1-5 (UNP residues 1-201) / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Organ: Blood / Tissue: Erythrocytes / References: UniProt: P16157

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Non-polymers , 3 types, 239 molecules

#4: Chemical ChemComp-CLR / CHOLESTEROL


Mass: 386.654 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H46O
#5: Chemical ChemComp-AJP / Digitonin


Mass: 1229.312 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C56H92O29 / Comment: detergent*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 235 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: Ankyrin complex mixture purified from digitonin-solubilized erythrocyte ghost membranes
Type: COMPLEX
Details: Particle set isolated by 3D classification from mixture mostly containing ankyrin complexes
Entity ID: #1-#3 / Source: NATURAL
Source (natural)Organism: Homo sapiens (human) / Cellular location: Plasma membrane / Organ: Blood / Tissue: Erythrocytes
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
IDNameVersionCategory
2Leginonimage acquisition
4cryoSPARC3CTF correction
7Coot0.9.8model fitting
9PHENIX1.20.1model refinement
10cryoSPARC3initial Euler assignment
11cryoSPARC3final Euler assignment
13cryoSPARC33D 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: 2.17 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 710437 / Symmetry type: POINT
Atomic model buildingProtocol: FLEXIBLE FIT / Space: REAL
Atomic model buildingPDB-ID: 4YZF

4yzf


Pdb chain-ID: A / Accession code: 4YZF / Source name: PDB / Type: experimental model
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 21.82 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00510419
ELECTRON MICROSCOPYf_angle_d0.75214183
ELECTRON MICROSCOPYf_dihedral_angle_d6.5051408
ELECTRON MICROSCOPYf_chiral_restr0.0431684
ELECTRON MICROSCOPYf_plane_restr0.0051726

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