6lfp

Cry3Aa protein for enzyme entrapment

spinqualitylabelsall models 6lfp, resolution 3.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lfp is a 1 chain structure with sequence from Bacillus thuringiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.31Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CR3AA_BACTD Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera. Publication Abstract from PubMed Cry3Aa is a protein that forms crystals naturally in the bacterium Bacillus thuringiensis. Here we report that coexpression of Cry3Aa and a Proteus mirabilis lipase without recombinant fusion results in the efficient passive entrapment of the lipase within the nanoporous channels of the resulting crystals. This Cry3Aa crystal-mediated entrapment provides multiple benefits to the lipase including a high enzyme loading, significantly improved thermostability, increased proteolytic resistance, and the ability to be utilized as a recyclable biodiesel catalyst. These characteristics, along with its greatly simplified method of isolation, highlight the potential of Cry3Aa crystal-mediated enzyme entrapment for use in biocatalysis and other biotechnological applications. In Vivo Enzyme Entrapment in a Protein Crystal.,Heater BS, Yang Z, Lee MM, Chan MK J Am Chem Soc. 2020 Jun 3;142(22):9879-9883. doi: 10.1021/jacs.9b13462. Epub 2020, May 19. PMID:32407637 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pesticidal crystal protein

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