8ZHS

Structure of Mbp-Bte1 fusion protein

Summary for 8ZHS

• Entry DOI: 10.2210/pdb8zhs/pdb
• Descriptor: Maltose/maltodextrin-binding periplasmic protein,N-terminal Bte1, C-terminal Bte1, GLYCEROL, ... (4 entities in total)
• Functional Keywords: antibacterial toxin, antitoxin
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 4
• Total formula weight: 138820.10

Authors

Xu, J.H.,Chen, Z.,Gao, X. (deposition date: 2024-05-11, release date: 2025-02-12, Last modification date: 2025-02-26)

Primary citation

Lim, B.,Xu, J.,Wierzbicki, I.H.,Gonzalez, C.G.,Chen, Z.,Gonzalez, D.J.,Gao, X.,Goodman, A.L.
A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.
Cell Host Microbe, 33:200-, 2025

PubMed Abstract: Antagonistic interactions play a key role in determining microbial community dynamics. Here, we report that one of the most widespread contact-dependent effectors in human gut microbiomes, Bte1, directly targets the PpiD-YfgM periplasmic chaperone complex in related microbes. Structural, biochemical, and genetic characterization of this interaction reveals that Bte1 reverses the activity of the chaperone complex, promoting substrate aggregation and toxicity. Using Bacteroides, we show that Bte1 is active in the mammalian gut, conferring a fitness advantage to expressing strains. Recipient cells targeted by Bte1 exhibit sensitivity to membrane-compromising conditions, and human gut microbes can use this effector to exploit pathogen-induced inflammation in the gut. Further, Bte1 allelic variation in gut metagenomes provides evidence for an arms race between Bte1-encoding and immunity-encoding strains in humans. Together, these studies demonstrate that human gut microbes alter the protein-folding capacity of neighboring cells and suggest strategies for manipulating community dynamics.

PubMed: 39909037
DOI: 10.1016/j.chom.2025.01.008

Experimental method

X-RAY DIFFRACTION (2.4 Å)