2es4

Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase

spinqualitylabelsall models 2es4, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2es4 is a 4 chain structure with sequence from Burkholderia glumae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: CA, CSO, IOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LIP_BURPL Catalyzes the hydrolysis of triacylglycerol. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lipase 3D Structures

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