6E6A

Triclinic crystal form of IncA G144A point mutant

Summary for 6E6A

• Entry DOI: 10.2210/pdb6e6a/pdb
• Descriptor: Inclusion membrane protein A, SODIUM ION (3 entities in total)
• Functional Keywords: membrane fusion, chlamydia, snare-like protein, inclusion, protein binding
• Biological source: Chlamydia trachomatis
• Total number of polymer chains: 2
• Total formula weight: 39216.21

Authors

Cingolani, G.,Paumet, F. (deposition date: 2018-07-24, release date: 2019-07-10, Last modification date: 2023-10-11)

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

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: 31227715
DOI: 10.1038/s41467-019-10806-9

Experimental method

X-RAY DIFFRACTION (1.95 Å)