Structure of a membrane-based steric chaperone in complex with its lipase substrate.
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.
Pauwels
Kris
K
Department of Molecular and Cellular Interactions, Flanders Interuniversity Institute for Biotechnology (VIB) and Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
Lustig
Ariel
A
Wyns
Lode
L
Tommassen
Jan
J
Savvides
Savvas N
SN
Van Gelder
Patrick
P
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D019117:Burkholderia / Q000201:enzymology; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism; D046912:Multiprotein Complexes; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013379:Substrate Specificity
D001426:Bacterial Proteins; C079999:LipA protein, Bacteria; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; D008049:Lipase; C504169:lipase foldase