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- PDB-5z0r: Structural insight into the Zika virus capsid encapsulating the v... -

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Basic information

Entry
Database: PDB / ID: 5z0r
TitleStructural insight into the Zika virus capsid encapsulating the viral genome
ComponentsExtracellular solute-binding protein family 1,viral genome protein
KeywordsVIRAL PROTEIN / Zika virus capsid
Function / homology
Function and homology information


detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / ATP-binding cassette (ABC) transporter complex ...detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / ATP-binding cassette (ABC) transporter complex / ribonucleoside triphosphate phosphatase activity / cell chemotaxis / viral capsid / double-stranded RNA binding / outer membrane-bounded periplasmic space / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / periplasmic space / host cell endoplasmic reticulum membrane / protein dimerization activity / symbiont entry into host cell / RNA-dependent RNA polymerase activity / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / DNA damage response / host cell nucleus / virion attachment to host cell / virion membrane / structural molecule activity / extracellular region / ATP binding / membrane / metal ion binding
Similarity search - Function
Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase ...Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / Flavivirus non-structural protein NS4A / Flavivirus NS2B domain profile. / mRNA cap 0 and cap 1 methyltransferase (EC 2.1.1.56 and EC 2.1.1.57) domain profile. / Flavivirus non-structural protein NS2A / Flavivirus non-structural protein NS2A / Envelope glycoprotein M, flavivirus / Flavivirus envelope glycoprotein M / Flavivirus NS3, petidase S7 / Peptidase S7, Flavivirus NS3 serine protease / Flavivirus NS3 protease (NS3pro) domain profile. / RNA-directed RNA polymerase, flavivirus / Flavivirus RNA-directed RNA polymerase, fingers and palm domains / Flavivirus non-structural Protein NS1 / Flavivirus non-structural protein NS1 / Envelope glycoprotein M superfamily, flavivirus / Flavivirus polyprotein propeptide / Flavivirus polyprotein propeptide superfamily / Flavivirus polyprotein propeptide / Bacterial extracellular solute-binding protein / Flaviviral glycoprotein E, central domain, subdomain 1 / Flaviviral glycoprotein E, central domain, subdomain 2 / Flavivirus envelope glycoprotein E, Stem/Anchor domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain superfamily / Flavivirus glycoprotein central and dimerisation domain / Flavivirus glycoprotein, central and dimerisation domains / Ribosomal RNA methyltransferase, FtsJ domain / FtsJ-like methyltransferase / Bacterial extracellular solute-binding protein / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Flaviviral glycoprotein E, dimerisation domain / DEAD box, Flavivirus / Flavivirus DEAD domain / Immunoglobulin E-set / Superfamilies 1 and 2 helicase C-terminal domain profile. / Helicase, C-terminal / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
alpha-maltose / Maltodextrin-binding protein / Genome polyprotein / Maltose/maltodextrin-binding periplasmic protein
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å
AuthorsLi, T. / Zhao, Q. / Yang, X. / Chen, C. / Yang, K. / Wu, C. / Zhang, T. / Duan, Y. / Xue, X. / Mi, K. ...Li, T. / Zhao, Q. / Yang, X. / Chen, C. / Yang, K. / Wu, C. / Zhang, T. / Duan, Y. / Xue, X. / Mi, K. / Ji, X. / Wang, Z. / Yang, H.
Funding support China, 3items
OrganizationGrant numberCountry
National Key Basic Research Program of China2015CB859800 China
the National Natural Science Foundation of China31528006 China
the National Key Research Program of China2016YFD0500300 China
CitationJournal: Cell Res. / Year: 2018
Title: Structural insight into the Zika virus capsid encapsulating the viral genome.
Authors: Li, T. / Zhao, Q. / Yang, X. / Chen, C. / Yang, K. / Wu, C. / Zhang, T. / Duan, Y. / Xue, X. / Mi, K. / Ji, X. / Wang, Z. / Yang, H.
History
DepositionDec 20, 2017Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 11, 2018Provider: repository / Type: Initial release
Revision 1.1May 2, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / 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_molecule_features / pdbx_nonpoly_scheme / pdbx_validate_close_contact / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.type / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_atom_id_2 / _pdbx_validate_close_contact.auth_comp_id_2 / _pdbx_validate_close_contact.auth_seq_id_2
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Nov 22, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Extracellular solute-binding protein family 1,viral genome protein
B: Extracellular solute-binding protein family 1,viral genome protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)98,6394
Polymers97,9552
Non-polymers6852
Water6,720373
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6500 Å2
ΔGint-36 kcal/mol
Surface area36890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)74.301, 81.425, 77.190
Angle α, β, γ (deg.)90.00, 104.79, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Extracellular solute-binding protein family 1,viral genome protein


Mass: 48977.270 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: The fusion of MBP-TAG (UNP residues 27-395) and Zika virus capsid (UNP residues 24-98)
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: B / BL21-DE3, BL21(DE3) / Gene: ECBD_4002 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: A0A140NCD0, UniProt: A0A1D9C0W3, UniProt: P0AEX9*PLUS
#2: Polysaccharide alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 373 / 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: 2.3 Å3/Da / Density % sol: 46.63 %
Crystal growTemperature: 293 K / Method: microbatch / pH: 8.5
Details: 10% v/v 2-Propanol, 0.1 M BICINE pH 8.5, 30% w/v Polyethylene glycol 1500

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97791 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Sep 5, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97791 Å / Relative weight: 1
ReflectionResolution: 2.05→50 Å / Num. obs: 55737 / % possible obs: 94.7 % / Redundancy: 4.4 % / Net I/σ(I): 10.5
Reflection shellResolution: 2.05→2.09 Å

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575)refinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1EZ9, 1SFK

1ez9

1sfk


Resolution: 2.05→48.286 Å / SU ML: 0.28 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 27.6 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2537 1912 3.6 %RANDOM
Rwork0.2209 ---
obs0.2221 53145 95.05 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.05→48.286 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6879 0 46 373 7298
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0047087
X-RAY DIFFRACTIONf_angle_d1.0589605
X-RAY DIFFRACTIONf_dihedral_angle_d12.1672629
X-RAY DIFFRACTIONf_chiral_restr0.0451066
X-RAY DIFFRACTIONf_plane_restr0.0041224
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.05-2.10130.31431330.29863034X-RAY DIFFRACTION80
2.1013-2.15810.35581090.28673276X-RAY DIFFRACTION85
2.1581-2.22160.32451260.27343317X-RAY DIFFRACTION88
2.2216-2.29330.28491300.27583515X-RAY DIFFRACTION91
2.2933-2.37530.34481330.26723591X-RAY DIFFRACTION94
2.3753-2.47040.29661450.25943719X-RAY DIFFRACTION97
2.4704-2.58280.27041290.25653803X-RAY DIFFRACTION99
2.5828-2.71890.30451470.24453830X-RAY DIFFRACTION99
2.7189-2.88930.28121430.24963841X-RAY DIFFRACTION100
2.8893-3.11230.27171440.24933841X-RAY DIFFRACTION100
3.1123-3.42540.29711460.22093835X-RAY DIFFRACTION100
3.4254-3.92090.2071400.19523853X-RAY DIFFRACTION100
3.9209-4.93920.19721460.17923865X-RAY DIFFRACTION100
4.9392-48.29890.22431410.19283913X-RAY DIFFRACTION99

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