Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure reveals how Lif uses a novel alpha-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.
        
Representative scheme of Bacterial_lip_FamI.2 structure and an image from PDBsum server
Databases
PDB-Sum
2ES4 Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
2ES4Fold classification based on Structure-Structure alignment of Proteins - FSSP server