Download MendeleyCrystal structure of monomeric Amuc_1100 from Akkermansia muciniphila.
Mou, L., Peng, X., Chen, Y., Xiao, Q., Liao, H., Liu, M., Guo, L., Liu, Y., Zhang, X., Deng, D.(2020) Acta Crystallogr F Struct Biol Commun 76: 168-174
- PubMed: 32254050
- DOI: https://doi.org/10.1107/S2053230X20004124
- Primary Citation of Related Structures:
6KNY - PubMed Abstract:
Many human diseases, such as obesity and diabetes, show annual increases in prevalence and often involve intestinal microbes. One such probiotic bacterium, Akkermansia muciniphila, which was discovered a decade ago, has been reported to influence glucose homeostasis and to contribute to gut health. Amuc_1100, a functionally uncharacterized protein of A. muciniphila, was found to be a key active component in reducing the body weight of mice. Here, the crystal structure of Amuc_1100 (residues 31-317), referred to as Amuc_1100*, is reported at 2.1 Å resolution. Amuc_1100* has a similar fold to three proteins related to pilus formation, PilO, PilN and EpsL, indicating a similar function. Biochemical investigations further confirmed a monomeric state for the soluble region of Amuc_1100, which differs from the dimeric states of PilO, PilN and EpsL. This study provides a structural basis for the elucidation of the molecular mechanism of Amuc_1100.
Organizational Affiliation:
Division of Obstetrics, Key Laboratory of Birth Defects and Related Diseases of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University, Chengdu, Sichuan 610041, People's Republic of China.
