期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-10806-9
关键词
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资金
- NIH [AI073486, AI144081, GM100888, AI121354, P30-GM110758, P50AI150481]
- NSF [1560325]
- NCI Cancer Center Support Grant [P30 CA56036, S10 OD017987]
- National Science Foundation [ACI-1548562]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1560325] Funding Source: National Science Foundation
Many intracellular bacteria, including Chlamydia, establish a parasitic membrane-bound organelle inside the host cell that is essential for the bacteria's survival. Chlamydia trachomatis forms inclusions that are decorated with poorly characterized membrane proteins known as Incs. The prototypical Inc, called IncA, enhances Chlamydia pathogenicity by promoting the homotypic fusion of inclusions and shares structural and functional similarity to eukaryotic SNAREs. Here, we present the atomic structure of the cytoplasmic domain of IncA, which reveals a non-canonical four-helix bundle. Structure-based mutagenesis, molecular dynamics simulation, and functional cellular assays identify an intramolecular clamp that is essential for IncA-mediated homotypic membrane fusion during infection.
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