Patrick van Gelder, Laboratory for Protein Biochemistry & Engineering, Ghent University, Belgium
Secretion via the type II secretion pathway in Gram-negative bacteria often relies critically on steric chaperones in the periplasm. A classic example of such chaperones is the lipase-specific foldase (Lif), a monotopic inner-membrane protein, representing a unique class of steric chaperones. Here, we report the crystal structure of Lif from Burkholderia glumae, a prototype for this class of chaperones, in complex with its cognate lipase. The structure reveals how Lif employs a novel a-helical scaffold to engulf lipase thereby creating an unusually extensive folding platform. In addition, folding studies of the lipase point to an intriguing folding fingerprint consisting of at least two well-spaced intermediates along the folding pathway. Taken together, our studies suggest that Lif and its cognate lipase represent a novel system designed to accommodate complex folding profiles.
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