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- EMDB-5317: FcRY dimer -

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Basic information

Entry
Database: EMDB / ID: EMD-5317
TitleFcRY dimer
Map dataThis is the cryoEM map of FcRY dimer.
Sample
  • Sample: FcRY
  • Protein or peptide: FcRY
Keywordsavian Fc receptor dimer
Biological speciesGallus gallus (chicken)
Methodsingle particle reconstruction / cryo EM / negative staining / Resolution: 28.0 Å
AuthorsHe Y / Bjorkman PJ
CitationJournal: Proc Natl Acad Sci U S A / Year: 2011
Title: Structure of FcRY, an avian immunoglobulin receptor related to mammalian mannose receptors, and its complex with IgY.
Authors: Yongning He / Pamela J Bjorkman /
Abstract: Fc receptors transport maternal antibodies across epithelial cell barriers to passively immunize newborns. FcRY, the functional counterpart of mammalian FcRn (a major histocompatibility complex ...Fc receptors transport maternal antibodies across epithelial cell barriers to passively immunize newborns. FcRY, the functional counterpart of mammalian FcRn (a major histocompatibility complex homolog), transfers IgY across the avian yolk sac, and represents a new class of Fc receptor related to the mammalian mannose receptor family. FcRY and FcRn bind immunoglobulins at pH ≤6.5, but not pH ≥7, allowing receptor-ligand association inside intracellular vesicles and release at the pH of blood. We obtained structures of monomeric and dimeric FcRY and an FcRY-IgY complex and explored FcRY's pH-dependent binding mechanism using electron cryomicroscopy (cryoEM) and small-angle X-ray scattering. The cryoEM structure of FcRY at pH 6 revealed a compact double-ring "head," in which the N-terminal cysteine-rich and fibronectin II domains were folded back to contact C-type lectin-like domains 1-6, and a "tail" comprising C-type lectin-like domains 7-8. Conformational changes at pH 8 created a more elongated structure that cannot bind IgY. CryoEM reconstruction of FcRY dimers at pH 6 and small-angle X-ray scattering analysis at both pH values confirmed both structures. The cryoEM structure of the FcRY-IgY revealed symmetric binding of two FcRY heads to the dimeric FcY, each head contacting the C(H)4 domain of one FcY chain. FcRY shares structural properties with mannose receptor family members, including a head and tail domain organization, multimerization that may regulate ligand binding, and pH-dependent conformational changes. Our results facilitate understanding of immune recognition by the structurally related mannose receptor family and comparison of diverse methods of Ig transport across evolution.
History
DepositionJun 30, 2011-
Header (metadata) releaseOct 26, 2011-
Map releaseOct 27, 2011-
UpdateOct 27, 2011-
Current statusOct 27, 2011Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 3.5
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 3.5
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_5317_1.png

Downloads & links

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Map

FileDownload / File: emd_5317.map.gz / Format: CCP4 / Size: 670.9 KB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThis is the cryoEM map of FcRY dimer.
Voxel sizeX=Y=Z: 4.24 Å
Density
Contour LevelBy AUTHOR: 3.5 / Movie #1: 3.5
Minimum - Maximum-0.595648 - 4.04315
Average (Standard dev.)0.0000000047407 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions565656
Spacing565656
CellA=B=C: 237.44 Å
α=β=γ: 90 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z4.244.244.24
M x/y/z565656
origin x/y/z0.0000.0000.000
length x/y/z237.440237.440237.440
α/β/γ90.00090.00090.000
start NX/NY/NZ-62-62-62
NX/NY/NZ125125125
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS565656
D min/max/mean-0.5964.0430.000

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Supplemental data

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Sample components

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Entire : FcRY

EntireName: FcRY
Components
  • Sample: FcRY
  • Protein or peptide: FcRY

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Supramolecule #1000: FcRY

SupramoleculeName: FcRY / type: sample / ID: 1000 / Oligomeric state: dimer / Number unique components: 1
Molecular weightExperimental: 360 KDa

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Macromolecule #1: FcRY

MacromoleculeName: FcRY / type: protein_or_peptide / ID: 1 / Name.synonym: FcRY / Number of copies: 2 / Oligomeric state: dimer / Recombinant expression: Yes
Source (natural)Organism: Gallus gallus (chicken) / synonym: chcken
Molecular weightExperimental: 180 KDa
Recombinant expressionOrganism: insect cell (unknown) / Recombinant plasmid: pVL1392

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Experimental details

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Structure determination

Methodnegative staining, cryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration2 mg/mL
BufferpH: 6 / Details: 50 mM Tris, 150 mM NaCl
StainingType: NEGATIVE / Details: cryo
VitrificationCryogen name: NITROGEN / Chamber humidity: 100 % / Chamber temperature: 77 K / Instrument: OTHER / Details: Vitrification instrument: FEI vitrobot

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Electron microscopy

MicroscopeFEI POLARA 300
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 50000
Specialist opticsEnergy filter - Name: Gatan
Sample stageSpecimen holder: eucentric / Specimen holder model: OTHER
TemperatureAverage: 77 K
Image recordingCategory: CCD / Film or detector model: GATAN ULTRASCAN 1000 (2k x 2k) / Digitization - Sampling interval: 4.24 µm / Average electron dose: 20 e/Å2
Experimental equipment
Model: Tecnai Polara / Image courtesy: FEI Company

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Image processing

Final reconstructionResolution.type: BY AUTHOR / Resolution: 28.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: EMAN, Frealign / Number images used: 1883

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