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- PDB-3j24: CryoEM reconstruction of complement decay-accelerating factor -

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Entry
Database: PDB / ID: 3j24
TitleCryoEM reconstruction of complement decay-accelerating factor
ComponentsComplement decay-accelerating factor
KeywordsIMMUNE SYSTEM / blood group antigen / complement pathway / glycoprotein / GPI-anchor / immune response / innate immunity / lipoprotein / membrane / Sushi
Function / homology
Function and homology information


regulation of lipopolysaccharide-mediated signaling pathway / negative regulation of complement activation / positive regulation of CD4-positive, alpha-beta T cell activation / respiratory burst / positive regulation of CD4-positive, alpha-beta T cell proliferation / regulation of complement-dependent cytotoxicity / ficolin-1-rich granule membrane / transport vesicle / anchored component of membrane / endoplasmic reticulum-Golgi intermediate compartment membrane ...regulation of lipopolysaccharide-mediated signaling pathway / negative regulation of complement activation / positive regulation of CD4-positive, alpha-beta T cell activation / respiratory burst / positive regulation of CD4-positive, alpha-beta T cell proliferation / regulation of complement-dependent cytotoxicity / ficolin-1-rich granule membrane / transport vesicle / anchored component of membrane / endoplasmic reticulum-Golgi intermediate compartment membrane / secretory granule membrane / complement activation, classical pathway / regulation of complement activation / positive regulation of T cell cytokine production / virus receptor activity / endoplasmic reticulum to Golgi vesicle-mediated transport / positive regulation of cytosolic calcium ion concentration / lipid binding / Golgi membrane / membrane raft / innate immune response / neutrophil degranulation / cell surface / extracellular exosome / extracellular region / plasma membrane
Sushi repeat (SCR repeat) / Sushi/SCR/CCP superfamily / Sushi/SCR/CCP domain
Complement decay-accelerating factor
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 9 Å
AuthorsYoder, J.D. / Hafenstein, S.H.
CitationJournal: J Virol / Year: 2012
Title: The crystal structure of a coxsackievirus B3-RD variant and a refined 9-angstrom cryo-electron microscopy reconstruction of the virus complexed with decay-accelerating factor (DAF) provide a ...Title: The crystal structure of a coxsackievirus B3-RD variant and a refined 9-angstrom cryo-electron microscopy reconstruction of the virus complexed with decay-accelerating factor (DAF) provide a new footprint of DAF on the virus surface.
Authors: Joshua D Yoder / Javier O Cifuente / Jieyan Pan / Jeffrey M Bergelson / Susan Hafenstein /
Abstract: The coxsackievirus-adenovirus receptor (CAR) and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). The first described DAF-binding isolate was ...The coxsackievirus-adenovirus receptor (CAR) and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). The first described DAF-binding isolate was obtained during passage of the prototype strain, Nancy, on rhabdomyosarcoma (RD) cells, which express DAF but very little CAR. Here, the structure of the resulting variant, CVB3-RD, has been solved by X-ray crystallography to 2.74 Å, and a cryo-electron microscopy reconstruction of CVB3-RD complexed with DAF has been refined to 9.0 Å. This new high-resolution structure permits us to correct an error in our previous view of DAF-virus interactions, providing a new footprint of DAF that bridges two adjacent protomers. The contact sites between the virus and DAF clearly encompass CVB3-RD residues recently shown to be required for binding to DAF; these residues interact with DAF short consensus repeat 2 (SCR2), which is known to be essential for virus binding. Based on the new structure, the mode of the DAF interaction with CVB3 differs significantly from the mode reported previously for DAF binding to echoviruses.
Validation Report
SummaryFull reportAbout validation report
History
DepositionAug 17, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 26, 2012Provider: repository / Type: Initial release
Revision 1.1Nov 14, 2012Group: Database references
Revision 1.2Jul 18, 2018Group: Data collection / Category: em_software / Item: _em_software.image_processing_id / _em_software.name

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Structure visualization

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  • Biological unit as complete icosahedral assembly
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  • Biological unit as icosahedral pentamer
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  • Biological unit as icosahedral 23 hexamer
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  • Deposited structure unit
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  • Simplified surface model + fitted atomic model
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Structure viewerMolecule:
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Assembly

Deposited unit
B: Complement decay-accelerating factor


Theoretical massNumber of molelcules
Total (without water)28,1751
Polymers28,1751
Non-polymers00
Water0
1
B: Complement decay-accelerating factor
x 60


Theoretical massNumber of molelcules
Total (without water)1,690,48060
Polymers1,690,48060
Non-polymers00
Water0
TypeNameSymmetry operationNumber
point symmetry operation60
2


  • Idetical with deposited unit in distinct coordinate
  • icosahedral asymmetric unit
TypeNameSymmetry operationNumber
point symmetry operation1
3
B: Complement decay-accelerating factor
x 5


  • icosahedral pentamer
  • 141 kDa, 5 polymers
Theoretical massNumber of molelcules
Total (without water)140,8735
Polymers140,8735
Non-polymers00
Water0
TypeNameSymmetry operationNumber
point symmetry operation5
4
B: Complement decay-accelerating factor
x 6


  • icosahedral 23 hexamer
  • 169 kDa, 6 polymers
Theoretical massNumber of molelcules
Total (without water)169,0486
Polymers169,0486
Non-polymers00
Water0
TypeNameSymmetry operationNumber
point symmetry operation6
5


  • Idetical with deposited unit in distinct coordinate
  • icosahedral asymmetric unit, std point frame
TypeNameSymmetry operationNumber
transform to point frame1
SymmetryPoint symmetry: (Schoenflies symbol: I (icosahedral))

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Components

#1: Protein Complement decay-accelerating factor


Mass: 28174.666 Da / Num. of mol.: 1
Fragment: four extracellular SCR domains (UNP residues 35-285)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CD55, CR, DAF / Production host: Escherichia coli (E. coli) / References: UniProt: P08174

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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: Complement decay-accelerating factor bound to coxsackievirus B3-RD strain
Type: VIRUS
Buffer solutionName: 2-(N-morpholino)ethanesulfonic acid (MES) / pH: 6 / Details: 50mM MES
SpecimenConc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: Quantifoil
VitrificationInstrument: HOMEMADE PLUNGER / Cryogen name: ETHANE / Temp: 120 K
Details: Blotted before plunging in liquid ethane (homemade plunger).

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Electron microscopy imaging

MicroscopyModel: FEI/PHILIPS CM300FEG/T / Date: Aug 4, 2006
Electron gunElectron source: TUNGSTEN HAIRPIN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 45000 X / Calibrated magnification: 47000 X / Nominal defocus max: 4600 nm / Nominal defocus min: 1000 nm / Cs: 2 mm
Specimen holderModel: GATAN LIQUID NITROGEN / Specimen holder type: Side mounted nitrogen cooled / Temperature: 93 K / Temperature (max): 93 K / Temperature (min): 83 K / Tilt angle max: 0 ° / Tilt angle min: 0 °
Image recordingElectron dose: 24 e/Å2 / Film or detector model: KODAK SO-163 FILM
Image scansNum. digital images: 36
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

EM software
IDNameCategory
1CTFFINDCTF correction
2UCSF Chimeramodel fitting
3autoppparticle selection
4RobEMparticle selection
5Auto3DEM3D reconstruction
CTF correctionDetails: AUTO3DEM
SymmetryPoint symmetry: I (icosahedral)
3D reconstructionMethod: common lines / Resolution: 9 Å / Num. of particles: 3010 / Nominal pixel size: 2.94 Å / Actual pixel size: 2.94 Å / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL / Target criteria: average map value
Details: METHOD--Local refinement, rigid body REFINEMENT PROTOCOL--rigid body
Atomic model buildingPDB-ID: 1OJW
Pdb chain-ID: B
Refinement stepCycle: LAST
ProteinNucleic acidLigandSolventTotal
Num. atoms1946 0 0 0 1946

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