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Molecular Basis of BioJ, a Unique Gatekeeper in Bacterial Biotin Synthesis
- Source :
- iScience, Vol 19, Iss , Pp 796-808 (2019)
- Publication Year :
- 2019
- Publisher :
- Elsevier, 2019.
-
Abstract
- Summary: 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. : Biological Sciences; Microbiology; Structural Biology Subject Areas: Biological Sciences, Microbiology, Structural Biology
- Subjects :
- Science
Subjects
Details
- Language :
- English
- ISSN :
- 25890042
- Volume :
- 19
- Issue :
- 796-808
- Database :
- Directory of Open Access Journals
- Journal :
- iScience
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.fa7d967e435947d69280b2d3922715da
- Document Type :
- article
- Full Text :
- https://doi.org/10.1016/j.isci.2019.08.028