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Crystal structure of monomeric Amuc_1100 from Akkermansia muciniphila
Author(s) -
Mou Luqiu,
Peng Xi,
Chen Yan,
Xiao Qingjie,
Liao Huijuan,
Liu Mingfeng,
Guo Li,
Liu Yang,
Zhang Xiaohu,
Deng Dong
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20004124
Subject(s) - akkermansia muciniphila , chemistry , monomer , akkermansia , biology , biochemistry , microbiology and biotechnology , gut flora , organic chemistry , fermentation , lactobacillus , polymer
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.