7b21 | pdb_00007b21

The X183 domain from Cellvibrio japonicus Cbp2D

spinqualitylabelsall models 7b21, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7b21 is a 1 chain structure with sequence from Celju. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, HEC, NA Gene: cbp2D, CJA_2616 (CELJU) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The release of glucose from lignocellulosic waste for subsequent fermentation into biofuels holds promise for securing humankind's future energy needs. The discovery of a set of copper dependent enzymes known as lytic polysaccharide monooxygenases (LPMOs) has galvanized new research in this area. LPMOs act by oxidatively introducing chain breaks into cellulose and other polysaccharides, boosting the ability of cellulases to act on the substrate. Although several proteins have been implicated as electron sources in fungal LPMO biochemistry, no equivalent bacterial LPMO electron donors have been previously identified, although the proteins Cbp2D and E from Cellvibrio japonicus have been implicated as potential candidates. Here we analyze a small c-type cytochrome (CjX183) present in Cellvibrio japonicus Cbp2D, and show that it can initiate bacterial CuII/I LPMO reduction and also activate LPMO-catalyzed cellulose-degradation. In the absence of cellulose, CjX183-driven reduction of the LPMO results in less H2O2 production from O2, and correspondingly less oxidative damage to the enzyme than when ascorbate is used as the reducing agent. Significantly, using CjX183 as the activator maintained similar cellulase boosting levels relative to the use of an equivalent amount of ascorbate. Our results therefore add further evidence to the impact that the choice of electron source can have on LPMO action. Furthermore, the study of Cbp2D and other similar proteins may yet reveal new insight into the redox processes governing polysaccharide degradation in bacteria. C-type cytochrome-initiated reduction of bacterial lytic polysaccharide monooxygenases.,Branch J, Rajagopal BS, Paradisi A, Yates N, Lindley PJ, Smith J, Hollingsworth K, Turnbull B, Henrissat B, Parkin A, Berry A, Hemsworth GR Biochem J. 2021 Jul 9. pii: 229228. doi: 10.1042/BCJ20210376. PMID:34240737 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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