5ACH

X-ray Structure of LPMO

Summary for 5ACH

• Entry DOI: 10.2210/pdb5ach/pdb
• Related: 5ACF 5ACG 5ACI 5ACJ
• Descriptor: LYTIC POLYSACCHARIDE MONOOXYGENASE, CHLORIDE ION, COPPER (II) ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, monooxygenase
• Biological source: LENTINUS SIMILIS
• Total number of polymer chains: 1
• Total formula weight: 26089.40

Authors

Frandsen, K.E.H.,Poulsen, J.N.,Tovborg, M.,Johansen, K.S.,Lo Leggio, L. (deposition date: 2015-08-17, release date: 2016-03-02, Last modification date: 2024-01-10)

Primary citation

Frandsen, K.E.,Simmons, T.J.,Dupree, P.,Poulsen, J.C.,Hemsworth, G.R.,Ciano, L.,Johnston, E.M.,Tovborg, M.,Johansen, K.S.,von Freiesleben, P.,Marmuse, L.,Fort, S.,Cottaz, S.,Driguez, H.,Henrissat, B.,Lenfant, N.,Tuna, F.,Baldansuren, A.,Davies, G.J.,Lo Leggio, L.,Walton, P.H.
The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases.
Nat. Chem. Biol., 12:298-303, 2016

PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and chitin. Since their discovery, LPMOs have become integral factors in the industrial utilization of biomass, especially in the sustainable generation of cellulosic bioethanol. We report here a structural determination of an LPMO-oligosaccharide complex, yielding detailed insights into the mechanism of action of these enzymes. Using a combination of structure and electron paramagnetic resonance spectroscopy, we reveal the means by which LPMOs interact with saccharide substrates. We further uncover electronic and structural features of the enzyme active site, showing how LPMOs orchestrate the reaction of oxygen with polysaccharide chains.

PubMed: 26928935
DOI: 10.1038/nchembio.2029

Experimental method

X-RAY DIFFRACTION (1.28 Å)