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 α-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.
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We acknowledge the use of synchrotron beam time at the European Molecular Biology Laboratory beamlines (Deutsches Elektronen-Synchrotron and European Synchrotron Radiation Facility). We thank G. Machaidze, U. Aebi and E. De Genst for help with analytical ultracentrifugation and surface plasmon resonance experiments, respectively, and L. Buts, K. Decanniere and R. Loris for useful discussions. K. Pauwels is supported by the Institute for the Promotion of Innovation by Science and Technology in Flanders. This research was sponsored by the European Commission-FP5 (QLRT-2001-02086).
The authors declare no competing financial interests.
Analytical gel filtration (PDF 65 kb)
Sequence alignment of selected members of the Lif superfamily and comparison with secondary structure elements in Lif from B. glumae (PDF 166 kb)
Near-UV CD spectra of Lif and native LipA (PDF 18 kb)
Sedimentation velocity and sedimentation equilibrium experiments of Lif and LipA (PDF 13 kb)
Data collection and crystallographic refinement statistics (PDF 42 kb)
Conserved residues of Lif interacting with conserved residues in LipA (PDF 16 kb)
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Pauwels, K., Lustig, A., Wyns, L. et al. Structure of a membrane-based steric chaperone in complex with its lipase substrate. Nat Struct Mol Biol 13, 374–375 (2006). https://doi.org/10.1038/nsmb1065
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