6K1T
The structure of Francisella virulence factor BioJ
Summary for 6K1T
| Entry DOI | 10.2210/pdb6k1t/pdb |
| Descriptor | Alpha/beta hydrolase fold family protein (2 entities in total) |
| Functional Keywords | virulence factor bioj, hydrolase |
| Biological source | Francisella philomiragia subsp. philomiragia ATCC 25015 |
| Total number of polymer chains | 1 |
| Total formula weight | 35479.43 |
| Authors | Ouyang, S.,Guan, H.,Zhang, S. (deposition date: 2019-05-12, release date: 2020-04-15, Last modification date: 2024-03-06) |
| Primary citation | Wei, W.,Guan, H.,Zhu, T.,Zhang, S.,Fan, C.,Ouyang, S.,Feng, Y. Molecular Basis of BioJ, a Unique Gatekeeper in Bacterial Biotin Synthesis. Iscience, 19:796-808, 2019 Cited by 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. PubMed: 31494495DOI: 10.1016/j.isci.2019.08.028 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.584 Å) |
Structure validation
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