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Nature Research, Nature Structural and Molecular Biology, 4(13), p. 374-375, 2006

DOI: 10.1038/nsmb1065

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Structure of a membrane-based steric chaperone in complex with its lipase substrate

Journal article published in 2006 by Kris Pauwels ORCID, Ariel Lustig, Lode Wyns, Jan Tommassen, Savvas N. Savvides, Patrick Van Gelder
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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.