6X80

Structure of the Campylobacter jejuni G508A Flagellar Filament


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.50 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: HELICAL 

wwPDB Validation   3D Report Full Report


This is version 2.3 of the entry. See complete history


Literature

Atomic structure of the Campylobacter jejuni flagellar filament reveals how epsilon Proteobacteria escaped Toll-like receptor 5 surveillance.

Kreutzberger, M.A.B.Ewing, C.Poly, F.Wang, F.Egelman, E.H.

(2020) Proc Natl Acad Sci U S A 117: 16985-16991

  • DOI: https://doi.org/10.1073/pnas.2010996117
  • Primary Citation of Related Structures:  
    6X80

  • PubMed Abstract: 

    Vertebrates, from zebra fish to humans, have an innate immune recognition of many bacterial flagellins. This involves a conserved eight-amino acid epitope in flagellin recognized by the Toll-like receptor 5 (TLR5). Several important human pathogens, such as Helicobacter pylori and Campylobacter jejuni , have escaped TLR5 activation by mutations in this epitope. When such mutations were introduced into Salmonella flagellin, motility was abolished. It was previously argued, using very low-resolution cryoelectron microscopy (cryo-EM), that C. jejuni accommodated these mutations by forming filaments with 7 protofilaments, rather than the 11 found in other bacteria. We have now determined the atomic structure of the C. jejuni G508A flagellar filament from a 3.5-Å-resolution cryo-EM reconstruction, and show that it has 11 protofilaments. The residues in the C. jejuni TLR5 epitope have reduced contacts with the adjacent subunit compared to other bacterial flagellar filament structures. The weakening of the subunit-subunit interface introduced by the mutations in the TLR5 epitope is compensated for by extensive interactions between the outer domains of the flagellin subunits. In other bacteria, these outer domains can be nearly absent or removed without affecting motility. Furthermore, we provide evidence for the stabilization of these outer domain interactions through glycosylation of key residues. These results explain the essential role of glycosylation in C. jejuni motility, and show how the outer domains have evolved to play a role not previously found in other bacteria.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Flagellin A
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V
576Campylobacter jejuniMutation(s): 1 
Gene Names: flaA
UniProt
Find proteins for P22251 (Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828))
Explore P22251 
Go to UniProtKB:  P22251
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22251
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
P8E (Subject of Investigation/LOI)
Query on P8E

Download Ideal Coordinates CCD File 
AA [auth A]
AB [auth B]
AC [auth D]
AD [auth E]
AE [auth G]
AA [auth A],
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AC [auth D],
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AG [auth J],
AH [auth K],
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AM [auth S],
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PG [auth K],
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PJ [auth O],
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ZH [auth M],
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5,7-diamino-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-non-2-ulopyranosonic acid
C9 H18 N2 O6
ZFZFJUIKYIVPNP-YXGHPGITSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.50 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: HELICAL 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONSPIDER
RECONSTRUCTIONRELION

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesR35GM122510
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesT32GM080186

Revision History  (Full details and data files)

  • Version 1.0: 2020-07-08
    Type: Initial release
  • Version 2.0: 2020-07-29
    Changes: Advisory, Atomic model, Data collection, Derived calculations
  • Version 2.1: 2021-10-06
    Changes: Database references
  • Version 2.2: 2022-04-27
    Changes: Structure summary
  • Version 2.3: 2024-05-15
    Changes: Data collection