8BFL

Jumbo Phage phi-kp24 empty capsid hexamers

  • Classification: VIRUS
  • Organism(s): Klebsiella phage vB_KpM_FBKp24
  • Mutation(s): No 

  • Deposited: 2022-10-26 Released: 2022-12-07 
  • Deposition Author(s): Ouyang, R.
  • Funding Organization(s): Netherlands Organisation for Scientific Research (NWO)

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers.

Ouyang, R.Costa, A.R.Cassidy, C.K.Otwinowska, A.Williams, V.C.J.Latka, A.Stansfeld, P.J.Drulis-Kawa, Z.Briers, Y.Pelt, D.M.Brouns, S.J.J.Briegel, A.

(2022) Nat Commun 13: 7241-7241

  • DOI: https://doi.org/10.1038/s41467-022-34972-5
  • Primary Citation of Related Structures:  
    8AU1, 8BFK, 8BFL, 8BFP

  • PubMed Abstract: 

    The Klebsiella jumbo myophage ϕKp24 displays an unusually complex arrangement of tail fibers interacting with a host cell. In this study, we combine cryo-electron microscopy methods, protein structure prediction methods, molecular simulations, microbiological and machine learning approaches to explore the capsid, tail, and tail fibers of ϕKp24. We determine the structure of the capsid and tail at 4.1 Å and 3.0 Å resolution. We observe the tail fibers are branched and rearranged dramatically upon cell surface attachment. This complex configuration involves fourteen putative tail fibers with depolymerase activity that provide ϕKp24 with the ability to infect a broad panel of capsular polysaccharide (CPS) types of Klebsiella pneumoniae. Our study provides structural and functional insight into how ϕKp24 adapts to the variable surfaces of capsulated bacterial pathogens, which is useful for the development of phage therapy approaches against pan-drug resistant K. pneumoniae strains.


  • Organizational Affiliation

    MOE Key Laboratory for Nonequilibrium Synthesis and Modulation of Condensed Matter, School of Physics, Xi'an Jiaotong University, Xianning West Road 28, Xi'an, 710049, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major head protein570Klebsiella phage vB_KpM_FBKp24Mutation(s): 0 
UniProt
Find proteins for A0A7U0GBA8 (Klebsiella phage vB_KpM_FBKp24)
Explore A0A7U0GBA8 
Go to UniProtKB:  A0A7U0GBA8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A7U0GBA8
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.10 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data

  • Released Date: 2022-12-07 
  • Deposition Author(s): Ouyang, R.

Funding OrganizationLocationGrant Number
Netherlands Organisation for Scientific Research (NWO)Netherlands84.034.014

Revision History  (Full details and data files)

  • Version 1.0: 2022-12-07
    Type: Initial release