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- PDB-6pw2: Structural Basis for Cooperative Binding of EBNA1 to the Epstein-... -

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Basic information

Entry
Database: PDB / ID: 6pw2
TitleStructural Basis for Cooperative Binding of EBNA1 to the Epstein-Barr Virus Dyad Symmetry Minimal Origin of Replication
Components
  • DNA (62-MER)
  • DNA (62-MER) complementary DNA strand
  • Epstein-Barr nuclear antigen 1
Keywordsviral protein/dna / EBNA1 / DNA binding protein / Epstein-Barr Virus / viral protein / viral protein-dna complex
Function / homology
Function and homology information


host cell PML body / viral latency / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 5'-phosphomonoesters / symbiont-mediated disruption of host cell PML body / regulation of DNA replication / enzyme-substrate adaptor activity / endonuclease activity / symbiont-mediated suppression of host NF-kappaB cascade / DNA-binding transcription factor activity / positive regulation of DNA-templated transcription / DNA binding
Similarity search - Function
Epstein Barr virus nuclear antigen-1, DNA-binding domain / Epstein Barr virus nuclear antigen-1, DNA-binding / Epstein Barr virus nuclear antigen-1, DNA-binding domain / Epstein Barr virus nuclear antigen-1, DNA-binding domain superfamily / E2/EBNA1, C-terminal / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
DNA / DNA (> 10) / Epstein-Barr nuclear antigen 1
Similarity search - Component
Biological speciesEpstein-Barr virus (Epstein-Barr virus)
Human herpesvirus 4 strain B95-8 (Epstein-Barr virus (strain B95-8))
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.01 Å
AuthorsMessick, T.E. / Malecka, K.A. / Lieberman, P.M.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Wellcome TrustWT096496 United Kingdom
CitationJournal: J.Virol. / Year: 2019
Title: Structural Basis for Cooperative Binding of EBNA1 to the Epstein-Barr Virus Dyad Symmetry Minimal Origin of Replication.
Authors: Malecka, K.A. / Dheekollu, J. / Deakyne, J.S. / Wiedmer, A. / Ramirez, U.D. / Lieberman, P.M. / Messick, T.E.
History
DepositionJul 22, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 28, 2019Provider: repository / Type: Initial release
Revision 1.1Oct 9, 2019Group: Data collection / Database references / Category: citation / Item: _citation.journal_abbrev / _citation.journal_volume
Revision 1.2Oct 11, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _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: Epstein-Barr nuclear antigen 1
B: Epstein-Barr nuclear antigen 1
C: Epstein-Barr nuclear antigen 1
D: Epstein-Barr nuclear antigen 1
E: DNA (62-MER)
F: DNA (62-MER) complementary DNA strand
I: Epstein-Barr nuclear antigen 1
J: Epstein-Barr nuclear antigen 1
K: Epstein-Barr nuclear antigen 1
L: Epstein-Barr nuclear antigen 1
G: DNA (62-MER)
H: DNA (62-MER) complementary DNA strand


Theoretical massNumber of molelcules
Total (without water)204,49312
Polymers204,49312
Non-polymers00
Water724
1
A: Epstein-Barr nuclear antigen 1
B: Epstein-Barr nuclear antigen 1
C: Epstein-Barr nuclear antigen 1
D: Epstein-Barr nuclear antigen 1
E: DNA (62-MER)
F: DNA (62-MER) complementary DNA strand


Theoretical massNumber of molelcules
Total (without water)102,2476
Polymers102,2476
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area26210 Å2
ΔGint-143 kcal/mol
Surface area37500 Å2
MethodPISA
2
I: Epstein-Barr nuclear antigen 1
J: Epstein-Barr nuclear antigen 1
K: Epstein-Barr nuclear antigen 1
L: Epstein-Barr nuclear antigen 1
G: DNA (62-MER)
H: DNA (62-MER) complementary DNA strand


Theoretical massNumber of molelcules
Total (without water)102,2476
Polymers102,2476
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area26100 Å2
ΔGint-130 kcal/mol
Surface area34810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)64.118, 283.384, 63.899
Angle α, β, γ (deg.)90.000, 89.800, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

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Components

#1: Protein
Epstein-Barr nuclear antigen 1 / EBV nuclear antigen 1


Mass: 16008.498 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Epstein-Barr virus (strain B95-8) (Epstein-Barr virus (strain B95-8))
Strain: B95-8 / Gene: EBNA1, BKRF1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P03211
#2: DNA chain DNA (62-MER)


Mass: 19128.277 Da / Num. of mol.: 2 / Source method: obtained synthetically
Details: CTAACCCTAATTCAATAGCATATGTTACCCAACGGGAAGCATATGCTATCGAATTAGGGTTA
Source: (synth.) Human herpesvirus 4 strain B95-8 (Epstein-Barr virus (strain B95-8))
#3: DNA chain DNA (62-MER) complementary DNA strand


Mass: 19084.285 Da / Num. of mol.: 2 / Source method: obtained synthetically
Details: CTAACCCTAATTCAATAGCATATGTTACCCAACGGGAAGCATATGCTATCGAATTAGGGTTA
Source: (synth.) Human herpesvirus 4 strain B95-8 (Epstein-Barr virus (strain B95-8))
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 4 / 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: 3.02 Å3/Da / Density % sol: 59.27 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.75 / Details: 200 mM sodium malonate, 24% PEG 3350 / PH range: +/- 0.25 / Temp details: +/- 2 degrees

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Data collection

DiffractionMean temperature: 100 K / Ambient temp details: Cryostream / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 19, 2015
RadiationMonochromator: Si (111) Rosenbaum-Rock double-crystal monochromator
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 29088 / % possible obs: 99.6 % / Redundancy: 10.6 % / Rsym value: 0.159 / Net I/σ(I): 8.1
Reflection shellResolution: 3→3.05 Å / Redundancy: 8.5 % / Mean I/σ(I) obs: 0.16 / Num. unique obs: 2264 / Rsym value: 2.682 / % possible all: 98.7

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Processing

Software
NameClassification
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1B3T

1b3t


Resolution: 3.01→40.9 Å / Cross valid method: FREE R-VALUE
Details: TLS record as of below: tls = "chain 'A' and (resid 461 through 477 )" tls = "chain 'A' and (resid 478 through 491 )" tls = "chain 'A' and (resid 492 through 504 )" tls = "chain 'A' and ...Details: TLS record as of below: tls = "chain 'A' and (resid 461 through 477 )" tls = "chain 'A' and (resid 478 through 491 )" tls = "chain 'A' and (resid 492 through 504 )" tls = "chain 'A' and (resid 505 through 547 )" tls = "chain 'A' and (resid 548 through 560 )" tls = "chain 'A' and (resid 561 through 583 )" tls = "chain 'A' and (resid 584 through 599 )" tls = "chain 'A' and (resid 600 through 607 )" tls = "chain 'B' and (resid 461 through 477 )" tls = "chain 'B' and (resid 478 through 489 )" tls = "chain 'B' and (resid 490 through 513 )" tls = "chain 'B' and (resid 514 through 547 )" tls = "chain 'B' and (resid 548 through 560 )" tls = "chain 'B' and (resid 561 through 585 )" tls = "chain 'B' and (resid 586 through 607 )" tls = "chain 'C' and (resid 461 through 470 )" tls = "chain 'C' and (resid 471 through 477 )" tls = "chain 'C' and (resid 478 through 489 )" tls = "chain 'C' and (resid 490 through 513 )" tls = "chain 'C' and (resid 514 through 560 )" tls = "chain 'C' and (resid 561 through 568 )" tls = "chain 'C' and (resid 569 through 583 )" tls = "chain 'C' and (resid 584 through 607 )" tls = "chain 'D' and (resid 461 through 477 )" tls = "chain 'D' and (resid 478 through 537 )" tls = "chain 'D' and (resid 538 through 607 )" tls = "chain 'E' and (resid 3 through 17 )" tls = "chain 'E' and (resid 18 through 42 )" tls = "chain 'E' and (resid 43 through 57 )" tls = "chain 'E' and (resid 58 through 59 )" tls = "chain 'F' and (resid 5 through 24 )" tls = "chain 'F' and (resid 25 through 44 )" tls = "chain 'F' and (resid 45 through 54 )" tls = "chain 'F' and (resid 55 through 57 )" tls = "chain 'I' and (resid 461 through 477 )" tls = "chain 'I' and (resid 478 through 513 )" tls = "chain 'I' and (resid 514 through 537 )" tls = "chain 'I' and (resid 538 through 560 )" tls = "chain 'I' and (resid 561 through 599 )" tls = "chain 'I' and (resid 600 through 607 )" tls = "chain 'J' and (resid 461 through 478 )" tls = "chain 'J' and (resid 479 through 504 )" tls = "chain 'J' and (resid 505 through 537 )" tls = "chain 'J' and (resid 538 through 547 )" tls = "chain 'J' and (resid 548 through 560 )" tls = "chain 'J' and (resid 561 through 585 )" tls = "chain 'J' and (resid 586 through 599 )" tls = "chain 'J' and (resid 600 through 607 )" tls = "chain 'K' and (resid 461 through 477 )" tls = "chain 'K' and (resid 478 through 491 )" tls = "chain 'K' and (resid 492 through 513 )" tls = "chain 'K' and (resid 514 through 560 )" tls = "chain 'K' and (resid 561 through 568 )" tls = "chain 'K' and (resid 569 through 599 )" tls = "chain 'K' and (resid 600 through 607 )" tls = "chain 'L' and (resid 461 through 537 )" tls = "chain 'L' and (resid 538 through 607 )" tls = "chain 'G' and (resid 8 through 32 )" tls = "chain 'G' and (resid 33 through 52 )" tls = "chain 'G' and (resid 53 through 56 )" tls = "chain 'H' and (resid 7 through 21 )" tls = "chain 'H' and (resid 22 through 46 )" tls = "chain 'H' and (resid 47 through 55 )"
RfactorNum. reflection% reflectionSelection details
Rfree0.277 1977 -0.1
Rwork0.2199 ---
obs-28824 64.22 %-
Refinement stepCycle: LAST / Resolution: 3.01→40.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9000 4266 0 4 13270
LS refinement shell

Refine-ID: X-RAY DIFFRACTION

Resolution (Å)Rfactor RfreeNum. reflection Rfree% reflection Rfree (%)Rfactor RworkNum. reflection Rwork% reflection obs (%)
3.0114-3.1190.3794238.30.36292536
3.119-3.24380.3055305.20.314154613
3.2438-3.39130.2859807.90.284692923
3.3913-3.57010.36351096.50.2961156137
3.5701-3.79360.37252217.10.307289570
3.7936-4.08620.43252956.90.3087395995
4.0862-4.4970.279331670.19734191100
4.497-5.14660.24353006.70.17914145100
5.1466-6.480.223066.70.20364236100
6.48-40.87990.20472976.70.1704413299

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