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

Publication Type:

Journal Article

Authors:

Pauwels,K.; Lustig,A.; Wyns,L.; Tommassen,J.; Savvides,S.N.; Van,Gelder P.

Source:

Volume 13, Issue 4, p.374 - 375 (2006)

URL:

PM:16518399

Keywords:

Bacterial Proteins; chemistry; metabolism; Burkholderia; enzymology; Lipase; Models; Molecular; Molecular Chaperones; Multiprotein Complexes; Protein Folding; Protein Structure; Secondary; Substrate Specificity

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

Notes:

DA - 20060522
IS - 1545-9993 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Bacterial Proteins)
RN - 0 (LipA protein, Bacteria)
RN - 0 (Molecular Chaperones)
RN - 0 (Multiprotein Complexes)
RN - EC 3.1.1.3 (Lipase)
RN - EC 3.1.1.3 (lipase foldase)
SB - IM