6KNY

Structure of Amuc_1100 without transmembrane region from Akkermansia muciniphila

6KNY の概要

• エントリーDOI: 10.2210/pdb6kny/pdb
• 分子名称: Protein Amuc_1100 (2 entities in total)
• 機能のキーワード: uncharacterized, protein, unknown function
• 由来する生物種: Akkermansia muciniphila (strain ATCC BAA-835 / Muc)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62300.72

構造登録者

Mou, L.Q.,Xiao, Q.J.,Deng, D. (登録日: 2019-08-07, 公開日: 2020-04-15, 最終更新日: 2024-05-29)

主引用文献

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.,Sect.F, 76:168-174, 2020

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.

PubMed: 32254050
DOI: 10.1107/S2053230X20004124

実験手法

X-RAY DIFFRACTION (2.1 Å)