6E7E
High resolution crystal structure of IncA soluble domain
Summary for 6E7E
| Entry DOI | 10.2210/pdb6e7e/pdb |
| Descriptor | Inclusion membrane protein A (2 entities in total) |
| Functional Keywords | membrane fusion, chlamydia, snare-like protein, inclusion, protein binding |
| Biological source | Chlamydia trachomatis |
| Total number of polymer chains | 1 |
| Total formula weight | 19571.09 |
| Authors | Cingolani, G.,Paumet, F. (deposition date: 2018-07-26, release date: 2019-07-10, Last modification date: 2024-03-13) |
| Primary citation | Cingolani, G.,McCauley, M.,Lobley, A.,Bryer, A.J.,Wesolowski, J.,Greco, D.L.,Lokareddy, R.K.,Ronzone, E.,Perilla, J.R.,Paumet, F. Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA. Nat Commun, 10:2747-2747, 2019 Cited by PubMed Abstract: 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. PubMed: 31227715DOI: 10.1038/s41467-019-10806-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.12 Å) |
Structure validation
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