Work

Triclinic crystal form of IncA G144A point mutant

Year: 2018

Type: dataset

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.

Source: Worldwide Protein Data Bank

DOI: 10.2210/pdb6e6a/pdb

Authors: G. Cingolani, F. Paumet

Institutions: Thomas Jefferson University, Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies, National Research Council

Language: English

Topic: Cellular transport and secretion

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W2952291469

Cites: 50

Cited by: 14

Related to: 20