5a71

Open and closed conformations and protonation states of Candida antarctica Lipase B: atomic resolution native

spinqualitylabelsall models 5a71, resolution 0.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a71 is a 2 chain structure with sequence from Moesziomyces antarcticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.91Å Ligands: IPA, K, NA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LIPB_PSEA2 Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis. Publication Abstract from PubMed Lipases (E.C. 3.1.1.3) are ubiquitous hydrolases for the carboxyl ester bond of water-insoluble substrates such as triacylglycerols, phospholipids, and other insoluble substrates, acting in aqueous as well as in low-water media, thus being of considerable physiological significance with high interest also for their industrial applications. The hydrolysis reaction follows a two-step mechanism, or 'interfacial activation', with adsorption of the enzyme to an heterogeneous interface and subsequent enhancement of the lipolytic activity. Among lipases, Candida antarctica Lipase B (CALB) has never shown any significant interfacial activation, and a closed conformation of CALB has never been reported leading to the conclusion that its behaviour was due to the absence of a lid regulating the access to the active site. The lid open and closed conformations and their protonation states are observed in the crystal structure of CALB at 0.91 A resolution. Having the open and closed states at atomic resolution allows relating protonation to the conformation, indicating the role of Asp145 and Lys290 in the conformation alteration. The findings explain the lack of 'interfacial activation' of CALB and offer new elements to elucidate this mechanism, with the consequent implications for the catalytic properties and classification of lipases. Open and closed states of Candida antarctica Lipase B: protonation and the mechanism of interfacial activation.,Stauch B, Fisher SJ, Cianci M J Lipid Res. 2015 Oct 7. pii: jlr.M063388. PMID:26447231 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lipase 3D Structures

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