6F7E
NMR solution structure of the cellulose-binding family 2 carbohydrate binding domain (CBM2) from ScLPMO10C
Summary for 6F7E
| Entry DOI | 10.2210/pdb6f7e/pdb |
| NMR Information | BMRB: 27078 |
| Descriptor | Putative secreted cellulose binding protein (1 entity in total) |
| Functional Keywords | cellulose binding, beta-sandwich fold, lytic polysaccharide monooxgynease, lpmo, carbohydrate |
| Biological source | Streptomyces coelicolor A3(2) |
| Total number of polymer chains | 1 |
| Total formula weight | 10662.51 |
| Authors | Courtade, G.,Forsberg, Z.,Eijsink, V.,Aachmann, F. (deposition date: 2017-12-08, release date: 2018-07-11, Last modification date: 2023-06-14) |
| Primary citation | Courtade, G.,Forsberg, Z.,Heggset, E.B.,Eijsink, V.G.H.,Aachmann, F.L. The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation. J.Biol.Chem., 293:13006-13015, 2018 Cited by PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of polysaccharides such as cellulose and chitin, a feature that makes them key tools in industrial biomass conversion processes. The catalytic domains of a considerable fraction of LPMOs and other carbohydrate-active enzymes (CAZymes) are tethered to carbohydrate-binding modules (CBMs) by flexible linkers. These linkers preclude X-ray crystallographic studies, and the functional implications of these modular assemblies remain partly unknown. Here, we used NMR spectroscopy to characterize structural and dynamic features of full-length modular LPMO10C from We observed that the linker is disordered and extended, creating distance between the CBM and the catalytic domain and allowing these domains to move independently of each other. Functional studies with cellulose nanofibrils revealed that most of the substrate-binding affinity of full-length LPMO10C resides in the CBM. Comparison of the catalytic performance of full-length LPMO10C and its isolated catalytic domain revealed that the CBM is beneficial for LPMO activity at lower substrate concentrations and promotes localized and repeated oxidation of the substrate. Taken together, these results provide a mechanistic basis for understanding the interplay between catalytic domains linked to CBMs in LPMOs and CAZymes in general. PubMed: 29967065DOI: 10.1074/jbc.RA118.004269 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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