6KNY

Structure of Amuc_1100 without transmembrane region from Akkermansia muciniphila

Summary for 6KNY

• Entry DOI: 10.2210/pdb6kny/pdb
• Descriptor: Protein Amuc_1100 (2 entities in total)
• Functional Keywords: uncharacterized, protein, unknown function
• Biological source: Akkermansia muciniphila (strain ATCC BAA-835 / Muc)
• Total number of polymer chains: 2
• Total formula weight: 62300.72

Authors

Mou, L.Q.,Xiao, Q.J.,Deng, D. (deposition date: 2019-08-07, release date: 2020-04-15, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)