4OY7

Structure of cellulose active LPMO CelS2 (ScLPMO10C) in complex with Copper.

Summary for 4OY7

• Entry DOI: 10.2210/pdb4oy7/pdb
• Related: 4OY6 4OY8
• Descriptor: Putative secreted cellulose binding protein, COPPER (II) ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: lpmo, aa10, cbm33, pmo, gh61, cellulose degradation, copper monooxygenase, oxidoreductase
• Biological source: Streptomyces coelicolor
• Total number of polymer chains: 8
• Total formula weight: 168643.54

Authors

Forsberg, Z.,Mackenzie, A.K.,Sorlie, M.,Rohr, A.K.,Helland, R.,Arvai, A.S.,Vaaje-Kolstad, G.,Eijsink, V.G.H. (deposition date: 2014-02-11, release date: 2014-05-28, Last modification date: 2024-10-16)

Primary citation

Forsberg, Z.,Mackenzie, A.K.,Srlie, M.,Rhr, A.K.,Helland, R.,Arvai, A.S.,Vaaje-Kolstad, G.,Eijsink, V.G.
Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases.
Proc.Natl.Acad.Sci.USA, 111:8446-8451, 2014

PubMed Abstract: For decades, the enzymatic conversion of cellulose was thought to rely on the synergistic action of hydrolytic enzymes, but recent work has shown that lytic polysaccharide monooxygenases (LPMOs) are important contributors to this process. We describe the structural and functional characterization of two functionally coupled cellulose-active LPMOs belonging to auxiliary activity family 10 (AA10) that commonly occur in cellulolytic bacteria. One of these LPMOs cleaves glycosidic bonds by oxidation of the C1 carbon, whereas the other can oxidize both C1 and C4. We thus demonstrate that C4 oxidation is not confined to fungal AA9-type LPMOs. X-ray crystallographic structures were obtained for the enzyme pair from Streptomyces coelicolor, solved at 1.3 Å (ScLPMO10B) and 1.5 Å (CelS2 or ScLPMO10C) resolution. Structural comparisons revealed differences in active site architecture that could relate to the ability to oxidize C4 (and that also seem to apply to AA9-type LPMOs). Despite variation in active site architecture, the two enzymes exhibited similar affinities for Cu(2+) (12-31 nM), redox potentials (242 and 251 mV), and electron paramagnetic resonance spectra, with only the latter clearly different from those of chitin-active AA10-type LPMOs. We conclude that substrate specificity depends not on copper site architecture, but rather on variation in substrate binding and orientation. During cellulose degradation, the members of this LPMO pair act in synergy, indicating different functional roles and providing a rationale for the abundance of these enzymes in biomass-degrading organisms.

PubMed: 24912171
DOI: 10.1073/pnas.1402771111

Experimental method

X-RAY DIFFRACTION (1.5 Å)