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Crystal structure of monomeric Amuc_1100 from Akkermansia muciniphila.
Acta Crystallographica Section F ( IF 1.072 ) Pub Date : 2020-04-07 , DOI: 10.1107/s2053230x20004124
Luqiu Mou 1 , Xi Peng 1 , Yan Chen 2 , Qingjie Xiao 1 , Huijuan Liao 2 , Mingfeng Liu 2 , Li Guo 1 , Yang Liu 3 , Xiaohu Zhang 2 , Dong Deng 1
Affiliation  

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.

中文翻译:

得自Akkermansia muciniphila的单体Amuc_1100的晶体结构。

许多人类疾病,例如肥胖症和糖尿病,显示患病率逐年增加,并经常涉及肠道微生物。十年前就发现了一种这样的益生菌细菌Akkermansia muciniphila,它会影响葡萄糖体内稳态并有助于肠道健康。Amuc_1100,黏液曲霉的功能未知蛋白被发现是降低小鼠体重的关键活性成分。在这里,Amuc_1100(残基31-317)的晶体结构被称为Amuc_1100 *,其分辨率为2.1。Amuc_1100 *具有与菌毛形成相关的三种蛋白质PilO,PilN和EpsL相似的折叠,表明其功能相似。生化研究进一步证实了Amuc_1100可溶性区域的单体状态,该状态不同于PilO,PilN和EpsL的二聚状态。该研究为阐明Amuc_1100的分子机制提供了结构基础。
更新日期:2020-04-07
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