6K1T

The structure of Francisella virulence factor BioJ


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.58 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.208 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Molecular Basis of BioJ, a Unique Gatekeeper in Bacterial Biotin Synthesis.

Wei, W.Guan, H.Zhu, T.Zhang, S.Fan, C.Ouyang, S.Feng, Y.

(2019) iScience 19: 796-808

  • DOI: https://doi.org/10.1016/j.isci.2019.08.028
  • Primary Citation of Related Structures:  
    6K1T

  • PubMed Abstract: 

    Biotin is an indispensable cofactor in the three domains of life. The unusual virulence factor BioJ of Francisella catalyzes the formation of pimeloyl-ACP, an intermediate in biotin synthesis. Here, we report the 1.58 Å crystal structure of BioJ, the enzymatic activity of which is determined with the in vitro reconstituted reaction and biotin bioassay in vivo. Unlike the paradigm BioH, BioJ displays an atypical α/β-hydrolase fold. A structurally conserved catalytic triad (S151, D248, and H278) of BioJ is functionally defined. A proposed model for BioJ catalysis involves two basic residues-rich cavities, of which cavity-1, rather than cavity-2, binds to the ACP moiety of its physiological substrate, pimeloyl-ACP methyl ester. In summary, this finding provides molecular insights into the BioJ gatekeeper of biotin synthesis.


  • Organizational Affiliation

    Department of Pathogen Biology & Microbiology and General Intensive Care Unit of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China; College of Animal Science, Zhejiang University, Hangzhou 310058, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha/beta hydrolase fold family protein306Francisella philomiragia subsp. philomiragia ATCC 25015Mutation(s): 0 
Gene Names: BZ13_192
UniProt
Find proteins for C6YW90 (Francisella philomiragia subsp. philomiragia ATCC 25015)
Explore C6YW90 
Go to UniProtKB:  C6YW90
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC6YW90
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.58 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.208 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.943α = 90
b = 67.313β = 112.55
c = 55.571γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
autoPROCdata collection
autoPROCdata scaling
PHENIXphasing
Cootmodel building

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-04-15
    Type: Initial release
  • Version 1.1: 2024-03-06
    Changes: Data collection, Database references, Refinement description