4OPB
AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae
Summary for 4OPB
| Entry DOI | 10.2210/pdb4opb/pdb |
| Descriptor | Predicted protein, COPPER (II) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | metal binding protein |
| Biological source | Aspergillus oryzae (Yellow koji mold) |
| Total number of polymer chains | 1 |
| Total formula weight | 27120.38 |
| Authors | Lo Leggio, L.,Frandsen, K.H.,Davies, G.J.,Dupree, P.,Walton, P.,Henrissat, B.,Stringer, M.,Tovborg, M.,De Maria, L.,Johansen, K.S. (deposition date: 2014-02-05, release date: 2015-01-28, Last modification date: 2020-07-29) |
| Primary citation | Lo Leggio, L.,Simmons, T.J.,Poulsen, J.C.,Frandsen, K.E.,Hemsworth, G.R.,Stringer, M.A.,von Freiesleben, P.,Tovborg, M.,Johansen, K.S.,De Maria, L.,Harris, P.V.,Soong, C.L.,Dupree, P.,Tryfona, T.,Lenfant, N.,Henrissat, B.,Davies, G.J.,Walton, P.H. Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. Nat Commun, 6:5961-5961, 2015 Cited by PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are recently discovered enzymes that oxidatively deconstruct polysaccharides. LPMOs are fundamental in the effective utilization of these substrates by bacteria and fungi; moreover, the enzymes have significant industrial importance. We report here the activity, spectroscopy and three-dimensional structure of a starch-active LPMO, a representative of the new CAZy AA13 family. We demonstrate that these enzymes generate aldonic acid-terminated malto-oligosaccharides from retrograded starch and boost significantly the conversion of this recalcitrant substrate to maltose by β-amylase. The detailed structure of the enzyme's active site yields insights into the mechanism of action of this important class of enzymes. PubMed: 25608804DOI: 10.1038/ncomms6961 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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