6K1T

The structure of Francisella virulence factor BioJ

6K1T の概要

• エントリーDOI: 10.2210/pdb6k1t/pdb
• 分子名称: Alpha/beta hydrolase fold family protein (2 entities in total)
• 機能のキーワード: virulence factor bioj, hydrolase
• 由来する生物種: Francisella philomiragia subsp. philomiragia ATCC 25015
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35479.43

構造登録者

Ouyang, S.,Guan, H.,Zhang, S. (登録日: 2019-05-12, 公開日: 2020-04-15, 最終更新日: 2024-03-06)

主引用文献

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

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: 31494495
DOI: 10.1016/j.isci.2019.08.028

実験手法

X-RAY DIFFRACTION (1.584 Å)