Structural highlights
Function
LIP_BURPL Catalyzes the hydrolysis of triacylglycerol.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Frenken LG, Egmond MR, Batenburg AM, Bos JW, Visser C, Verrips CT. Cloning of the Pseudomonas glumae lipase gene and determination of the active site residues. Appl Environ Microbiol. 1992 Dec;58(12):3787-91. PMID:1476423 doi:10.1128/aem.58.12.3787-3791.1992
- ↑ Taipa MA, Liebeton K, Costa JV, Cabral JM, Jaeger KE. Lipase from Chromobacterium viscosum: biochemical characterization indicating homology to the lipase from Pseudomonas glumae. Biochim Biophys Acta. 1995 Jun 6;1256(3):396-402. PMID:7786905 doi:10.1016/0005-2760(95)00052-e
- ↑ 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
