5gnz | pdb_00005gnz

The M3 mutant structure of Bgl6

spinqualitylabelsall models 5gnz, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gnz is a 8 chain structure with sequence from Environmental sequence. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, GOL Related: 5gnx, 5gny Activity: Beta-glucosidase, with EC number 3.2.1.21 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Cellulose can be converted to ethanol via the fermentation of glucose, which is considered as a promising green alternative for transportation fuels. The conversion of cellulose to glucose needs three enzymes, in which beta-glucosidase (BGL) plays an essential role. However, BGL is inhibited by its own product glucose, greatly limiting its applications in industry. We previously obtained a novel BGL named Bgl6 with a high glucose tolerance. Further engineering through random mutagenesis produced a triple mutant M3 with improved thermostability. This enzyme shows promising properties for wide applications but the structural basis of the unusual properties of Bgl6 is not clear. In this study, we determined the crystal structures of Bgl6 and variants at high resolution, which provide insights into its glucose-tolerant mechanism and thermostability. Particularly, Bgl6 forms an extra channel that could be used as a secondary binding site for glucose, which may contribute to glucose tolerance. Additionally, the triple mutations could strengthen the hydrophobic interactions within the enzyme and may be responsible for the enhanced thermostability exhibited by M3, which was further confirmed by dynamic light scattering data. Lastly, structural comparison to other orthologs allows us to formulate new strategies on how to improve the catalytic efficiency of Bgl6. Structures of a glucose-tolerant beta-glucosidase provide insights into its mechanism.,Pang P, Cao LC, Liu YH, Xie W, Wang Z J Struct Biol. 2017 Feb 9. pii: S1047-8477(17)30017-5. doi:, 10.1016/j.jsb.2017.02.001. PMID:28189793 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-glucosidase 3D structures

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