Structural highlights
Function
[LIP_BURGL] Catalyzes the hydrolysis of triglycerides. [LIFO_BURGL] May be involved in the folding of the extracellular lipase during its passage through the periplasm.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of a membrane-based steric chaperone in complex with its lipase substrate.,Pauwels K, Lustig A, Wyns L, Tommassen J, Savvides SN, Van Gelder P Nat Struct Mol Biol. 2006 Apr;13(4):374-5. Epub 2006 Mar 5. PMID:16518399[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Frenken LG, de Groot A, Tommassen J, Verrips CT. Role of the lipB gene product in the folding of the secreted lipase of Pseudomonas glumae. Mol Microbiol. 1993 Aug;9(3):591-9. PMID:8412705
- ↑ Pauwels K, Lustig A, Wyns L, Tommassen J, Savvides SN, Van Gelder P. Structure of a membrane-based steric chaperone in complex with its lipase substrate. Nat Struct Mol Biol. 2006 Apr;13(4):374-5. Epub 2006 Mar 5. PMID:16518399 doi:10.1038/nsmb1065
