Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice.

ABSTRACT: Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and nutrients. We have reconstructed this 0.6-μm-long adhesin using a "dissect and build" structural biology approach and have established complementary roles for its five distinct regions. Domains in region I (RI) tether the adhesin to the type I secretion machinery in the periplasm of the bacterium and pass it through the outer membrane. RII comprises ~120 identical immunoglobulin-like β-sandwich domains that rigidify on binding Ca²⁺ to project the adhesion regions RIII and RIV i

SUBMITTER: Guo S 

PROVIDER: S-EPMC5550230 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature