9JG8
Structure of cargo complex (BtpeA-BtaeB-BtapC) bound to the VgrG spike from the Type VI secretion system
Summary for 9JG8
| Entry DOI | 10.2210/pdb9jg8/pdb |
| EMDB information | 61458 |
| Descriptor | DUF3289 family protein, Peptidase C39-like domain-containing protein, Bacteroides T6SS Adapter Protein C, ... (5 entities in total) |
| Functional Keywords | t6ss, co-delivery, effector complex, vgrg spike, antimicrobial protein |
| Biological source | Bacteroides fragilis More |
| Total number of polymer chains | 6 |
| Total formula weight | 372122.69 |
| Authors | Zheng, S.N.,Li, W.X.,Chen, Z.,Gao, X. (deposition date: 2024-09-06, release date: 2025-09-10, Last modification date: 2025-11-26) |
| Primary citation | Li, W.,Zheng, S.,Xu, X.,He, J.,Jiao, X.,Wang, M.,Hu, W.,Li, S.,Jiang, X.,Lim, B.,Shao, F.,Gao, X. A conserved adaptor orchestrates co-secretion of synergistic type VI effectors in gut Bacteroidota. Cell Host Microbe, 33:1901-, 2025 Cited by PubMed Abstract: Interbacterial competition is crucial for shaping microbial communities and is often mediated by type VI secretion systems (T6SSs) that inject effectors into competing bacteria. T6SS effectors are released via structural proteins such as VgrG, but the secretion timing and coordination are unclear. Here, we report two effectors, BtpeA (Bacteroides T6SS phosphatase effector A) and BtaeB (Bacteroides T6SS amidase effector B), within the Bacteroidota T6SS that exert distinct cell-wall destructive activities critical for interspecies competition but whose secretion is interdependent. BtpeA and BtaeB co-secretion requires an adaptor protein, BtapC (Bacteroides T6SS adaptor protein C), that mediates the sequential assembly of the pre-firing complex, VgrG-BtpeA-BtaeB-BtapC. Structural analyses of this quaternary complex elucidate multi-cargo loading mechanisms with a conserved loop in BtaeB serving as a "checkpoint" to ensure BtpeA co-secretion. During mouse colonization, the combined activities of BtpeA and BtaeB significantly exceed the sum of the individual effectors. These findings unveil a T6SS-mediated co-delivery mechanism that ensures functional synergism of effectors, highlighting potential applications in modulating gut microbiota. PubMed: 41072405DOI: 10.1016/j.chom.2025.09.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.06 Å) |
Structure validation
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