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- PDB-6rrs: T=3 MS2 Virus-like particle -

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Basic information

Entry
Database: PDB / ID: 6rrs
TitleT=3 MS2 Virus-like particle
ComponentsCapsid proteinCapsid
KeywordsVIRUS LIKE PARTICLE / MS2 / T=3 / BACTERIOPHAGE / VLP
Function / homology
Function and homology information


negative regulation of viral translation / T=3 icosahedral viral capsid / regulation of translation / structural molecule activity / RNA binding / identical protein binding
Similarity search - Function
MS2 Viral Coat Protein / MS2 Viral Coat Protein / Levivirus coat protein / Levivirus coat protein / Bacteriophage RNA-type, capsid / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesEscherichia phage MS2 (virus)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å
Authorsde Martin Garrido, N. / Ramlaul, K. / Simpson, P.A. / Crone, M.A. / Freemont, P.S. / Aylett, C.H.S.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Wellcome Trust206212_Z_17_Z United Kingdom
Royal Society206212_Z_17_Z United Kingdom
CitationJournal: Mol Microbiol / Year: 2020
Title: Bacteriophage MS2 displays unreported capsid variability assembling T = 4 and mixed capsids.
Authors: Natàlia de Martín Garrido / Michael A Crone / Kailash Ramlaul / Paul A Simpson / Paul S Freemont / Christopher H S Aylett /
Abstract: Bacteriophage MS2 is a positive-sense, single-stranded RNA virus encapsulated in an asymmetric T = 3 pseudo-icosahedral capsid. It infects Escherichia coli through the F-pilus, in which it binds ...Bacteriophage MS2 is a positive-sense, single-stranded RNA virus encapsulated in an asymmetric T = 3 pseudo-icosahedral capsid. It infects Escherichia coli through the F-pilus, in which it binds through a maturation protein incorporated into its capsid. Cryogenic electron microscopy has previously shown that its genome is highly ordered within virions, and that it regulates the assembly process of the capsid. In this study, we have assembled recombinant MS2 capsids with non-genomic RNA containing the capsid incorporation sequence, and investigated the structures formed, revealing that T = 3, T = 4 and mixed capsids between these two triangulation numbers are generated, and resolving structures of T = 3 and T = 4 capsids to 4 Å and 6 Å respectively. We conclude that the basic MS2 capsid can form a mix of T = 3 and T = 4 structures, supporting a role for the ordered genome in favouring the formation of functional T = 3 virions.
History
DepositionMay 20, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 8, 2020Provider: repository / Type: Initial release
Revision 1.1Jul 22, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name

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Structure visualization

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Assembly

Deposited unit
A: Capsid protein
B: Capsid protein
C: Capsid protein


Theoretical massNumber of molelcules
Total (without water)41,6093
Polymers41,6093
Non-polymers00
Water0
1
A: Capsid protein
B: Capsid protein
C: Capsid protein
x 60


Theoretical massNumber of molelcules
Total (without water)2,496,539180
Polymers2,496,539180
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1
point symmetry operation59
MethodPISA

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Components

#1: Protein Capsid protein / Capsid / CP / Coat protein


Mass: 13869.659 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia phage MS2 (virus) / Production host: Escherichia coli (E. coli) / References: UniProt: P03612

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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: Escherichia virus MS2Bacteriophage MS2 / Type: VIRUS / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Escherichia virus MS2
Source (recombinant)Organism: Escherichia coli (E. coli)
Details of virusEmpty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRUS-LIKE PARTICLE
Buffer solutionpH: 7.5 / Details: 10 mM Tris-HCl pH 7.5, 1 mM EDTA, 100 mM NaCl
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 278 K

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Electron microscopy imaging

Experimental equipment
Model: Tecnai F20 / Image courtesy: FEI Company
MicroscopyModel: FEI TECNAI F20
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 100000 X / Nominal defocus max: -2000 nm / Nominal defocus min: -300 nm / Cs: 2 mm / C2 aperture diameter: 50 µm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN
Specimen holder model: GATAN 626 SINGLE TILT LIQUID NITROGEN CRYO TRANSFER HOLDER
Image recordingAverage exposure time: 4 sec. / Electron dose: 80 e/Å2 / Film or detector model: FEI FALCON I (4k x 4k) / Num. of grids imaged: 4 / Num. of real images: 1040
Details: Frames were obtained with a beam-splitter and recorded at 100kx
Image scansSampling size: 14 µm / Width: 4096 / Height: 4096

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Processing

EM software
IDNameCategoryDetails
2EPUimage acquisition
4CTFFINDCTF correction
7UCSF Chimeramodel fitting
11RELIONclassificationVersion 2.1
12RELION3D reconstructionVersion 2.1
Image processingDetails: Dose weighting was applied with MotionCor2
CTF correctionDetails: Internal in RELION / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: I (icosahedral)
3D reconstructionResolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 899 / Algorithm: FOURIER SPACE
Details: Resolution within a tight mask was 3.9 by FSC 0.143 cut-off while unmasked resolution was 5.
Num. of class averages: 1 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL / Target criteria: Cross-correlation coefficient / Details: Dimers were fitted independently
Atomic model buildingPDB-ID: 5TC1

5tc1

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