8PHR

Middle part of the Borrelia bacteriophage BB1 procapsid, tenfold-symmetrized outer shell


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.65 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of the Borrelia Bacteriophage phi BB1 Procapsid.

Rumnieks, J.Fuzik, T.Tars, K.

(2023) J Mol Biol 435: 168323-168323

  • DOI: https://doi.org/10.1016/j.jmb.2023.168323
  • Primary Citation of Related Structures:  
    8PHO, 8PHP, 8PHQ, 8PHR, 8PHS, 8PHT, 8PHU, 8PKH, 8QO0, 8QO1

  • PubMed Abstract: 

    Bacteriophages of Borrelia burgdorferi are a biologically important but under-investigated feature of the Lyme disease-causing spirochete. No virulent borrelial viruses have been identified, but all B. burgdorferi isolates carry a prophage φBB1 as resident circular plasmids. Like its host, the φBB1 phage is quite distinctive and shares little sequence similarity with other known bacteriophages. We expressed φBB1 head morphogenesis proteins in Escherichia coli which resulted in assembly of homogeneous prolate procapsid structures and used cryo-electron microscopy to determine the three-dimensional structure of these particles. The φBB1 procapsids consist of 415 copies of the major capsid protein and an equal combined number of three homologous capsid decoration proteins that form trimeric knobs on the outside of the particle. One of the end vertices of the particle is occupied by a portal assembled from twelve copies of the portal protein. The φBB1 scaffolding protein is entirely α-helical and has an elongated shape with a small globular domain in the middle. Within the tubular section of the procapsid, the internal scaffold is built of stacked rings, each composed of 32 scaffolding protein molecules, which run in opposite directions from both caps with a heterogeneous part in the middle. Inside the portal-containing cap, the scaffold is organized asymmetrically with ten scaffolding protein molecules bound to the portal. The φBB1 procapsid structure provides better insight into the vast structural diversity of bacteriophages and presents clues of how elongated bacteriophage particles might be assembled.


  • Organizational Affiliation

    Latvian Biomedical Research and Study Center, Rātsupītes 1, 1067 Riga, Latvia. Electronic address: j.rumnieks@biomed.lu.lv.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major capsid protein319Borreliella burgdorferi B31Mutation(s): 0 
Gene Names: BB_L06
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Decorator protein P03185Borreliella burgdorferi B31Mutation(s): 0 
Gene Names: BB_L03
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Decorator protein P05EA [auth e],
F,
M,
X
190Borreliella burgdorferi B31Mutation(s): 0 
Gene Names: BbuZS7_P05
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Scaffold protein230Borreliella burgdorferi B31Mutation(s): 0 
Gene Names: BB_L02
UniProt
Find proteins for Q9R2Q2 (Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31))
Explore Q9R2Q2 
Go to UniProtKB:  Q9R2Q2
Entity Groups  
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UniProt GroupQ9R2Q2
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.65 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX1.20.1-4487
RECONSTRUCTIONRELION3.1.3

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
European Regional Development FundEuropean Union1.1.1.2/VIAA/4/20/704
iNEXT-DiscoveryEuropean Union18826
iNEXT-DiscoveryEuropean Union24421

Revision History  (Full details and data files)

  • Version 1.0: 2023-07-19
    Type: Initial release
  • Version 1.1: 2023-11-01
    Changes: Data collection, Database references
  • Version 1.2: 2023-11-15
    Changes: Database references