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- PDB-5jyj: Crystal structure of mouse JUNO -

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Basic information

Entry
Database: PDB / ID: 5jyj
TitleCrystal structure of mouse JUNO
ComponentsSperm-egg fusion protein Juno
KeywordsCELL ADHESION / Fertilization / Folate receptor
Function / homology
Function and homology information


Post-translational modification: synthesis of GPI-anchored proteins / sperm-egg recognition / fusion of sperm to egg plasma membrane involved in single fertilization / single fertilization / signaling receptor activity / cell adhesion / signaling receptor binding / membrane / plasma membrane
Similarity search - Function
Folate receptor / Folate receptor-like / Folate receptor family
Similarity search - Domain/homology
Sperm-egg fusion protein Juno
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsKato, K. / Nishimasu, H. / Morita, J. / Ishitani, R. / Nureki, O.
CitationJournal: To Be Published
Title: Crystal structure of the egg IZUMO1 receptor JUNO
Authors: Kato, K. / Satouh, Y. / Nishimasu, H. / Kurabayashi, A. / Morita, J. / Fujihara, Y. / Oji, A. / Ishitani, R. / Ikawa, M. / Nureki, O.
History
DepositionMay 14, 2016Deposition site: RCSB / Processing site: PDBJ
Revision 1.0May 24, 2017Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_special_symmetry / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_special_symmetry.label_asym_id / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Sperm-egg fusion protein Juno
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,9112
Polymers24,4871
Non-polymers4241
Water64936
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area460 Å2
ΔGint6 kcal/mol
Surface area10080 Å2
Unit cell
Length a, b, c (Å)42.396, 54.449, 87.145
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP22121
Components on special symmetry positions
IDModelComponents
11A-1136-

HOH

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Components

#1: Protein Sperm-egg fusion protein Juno / Folate receptor 4 / Folate receptor delta / FR-delta / Folate-binding protein 3 / IZUMO1 receptor protein JUNO


Mass: 24486.629 Da / Num. of mol.: 1 / Fragment: UNP residues 20-221 / Mutation: N73D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Izumo1r, Folbp3, Folr4, Juno / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9EQF4
#2: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 36 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.05 Å3/Da / Density % sol: 40.11 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8
Details: Ammonium phosphate dibasic, Imidazole, Sodium chloride

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL32XU / Wavelength: 1 Å
DetectorType: RAYONIX MX225HE / Detector: CCD / Date: Jan 25, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.3→46.2 Å / Num. obs: 9442 / % possible obs: 99.7 % / Redundancy: 5.9 % / Net I/σ(I): 11.2

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Processing

Software
NameVersionClassification
PHENIX(1.10_2155: ???)refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→46.177 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.61
RfactorNum. reflection% reflection
Rfree0.2332 492 5.21 %
Rwork0.2077 --
obs0.209 9441 100 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.3→46.177 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1561 0 28 36 1625
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0021684
X-RAY DIFFRACTIONf_angle_d0.582317
X-RAY DIFFRACTIONf_dihedral_angle_d16.1961016
X-RAY DIFFRACTIONf_chiral_restr0.04241
X-RAY DIFFRACTIONf_plane_restr0.005302
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3001-2.53150.25971260.25212166X-RAY DIFFRACTION100
2.5315-2.89780.24981160.22562207X-RAY DIFFRACTION100
2.8978-3.65070.23611190.20812232X-RAY DIFFRACTION100
3.6507-46.18590.21781310.18962344X-RAY DIFFRACTION100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
12.12360.90270.89624.1472-0.23472.056-0.2948-0.09830.61550.6588-0.2991-0.6632-0.95670.56360.15750.4369-0.1383-0.22930.4340.03490.443-3.9359-11.5353-9.5073
22.35970.66050.83061.4720.30771.1531-0.12410.8362-0.3746-0.00780.0351-0.3177-0.22650.436-0.4450.2788-0.1768-0.09020.72670.15280.6731-2.2745-10.4416-22.7196
31.8939-1.45250.40056.0319-3.73282.78270.05270.29120.1722-0.0551-0.2453-0.2906-0.16890.46410.25250.1504-0.06720.00430.27290.01340.1992-11.8558-10.6762-20.8838
45.6201-4.20690.24116.6328-1.22272.93560.18760.0336-0.5761-0.14880.0570.10520.00170.3911-0.10650.1079-0.0113-0.00160.2978-0.03960.3238-12.0655-25.1176-15.5686
52.6557-1.18171.39784.4792-1.94023.53830.14140.1862-0.1616-0.1753-0.05340.17160.09690.0987-0.07770.20130.014-0.00780.1809-0.00590.2376-20.0027-11.3333-25.2625
62.3148-2.414-0.01213.3244-1.87824.42610.0113-0.25150.25160.73310.0760.5567-0.7947-0.1050.15590.58590.10560.03050.3249-0.01510.2211-20.1536-13.813-3.793
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 24 through 57 )
2X-RAY DIFFRACTION2chain 'A' and (resid 58 through 75 )
3X-RAY DIFFRACTION3chain 'A' and (resid 76 through 109 )
4X-RAY DIFFRACTION4chain 'A' and (resid 110 through 126 )
5X-RAY DIFFRACTION5chain 'A' and (resid 127 through 205 )
6X-RAY DIFFRACTION6chain 'A' and (resid 206 through 228 )

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