6e6a | pdb_00006e6a

Triclinic crystal form of IncA G144A point mutant

spinqualitylabelsall models 6e6a, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6e6a is a 2 chain structure with sequence from Chlamydia trachomatis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function INCA_CHLTR Chlamydia replicate within an intracellular vacuole, termed an inclusion. IncA is probably involved in the homotypic fusion of inclusions.[UniProtKB:A0A0H3MD02] Publication Abstract from PubMed 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. Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA.,Cingolani G, McCauley M, Lobley A, Bryer AJ, Wesolowski J, Greco DL, Lokareddy RK, Ronzone E, Perilla JR, Paumet F Nat Commun. 2019 Jun 21;10(1):2747. doi: 10.1038/s41467-019-10806-9. PMID:31227715 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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