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Nat Struct Mol Biol. 2006 Apr;13(4):374-5. Epub 2006 Mar 5.

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

Author information

1
Department of Molecular and Cellular Interactions, Flanders Interuniversity Institute for Biotechnology (VIB) and Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.

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.

PMID:
16518399
DOI:
10.1038/nsmb1065
[Indexed for MEDLINE]

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