Structural highlights
Publication Abstract from PubMed
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 A 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.
Crystal 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 Acta Crystallogr F Struct Biol Commun. 2020 Apr 1;76(Pt 4):168-174. doi:, 10.1107/S2053230X20004124. Epub 2020 Apr 1. PMID:32254050[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mou L, Peng X, Chen Y, Xiao Q, Liao H, Liu M, Guo L, Liu Y, Zhang X, Deng D. Crystal structure of monomeric Amuc_1100 from Akkermansia muciniphila. Acta Crystallogr F Struct Biol Commun. 2020 Apr 1;76(Pt 4):168-174. doi:, 10.1107/S2053230X20004124. Epub 2020 Apr 1. PMID:32254050 doi:http://dx.doi.org/10.1107/S2053230X20004124
