4OPB

AA13 Lytic polysaccharide monooxygenase from Aspergillus oryzae

4OPB の概要

• エントリーDOI: 10.2210/pdb4opb/pdb
• 分子名称: Predicted protein, COPPER (II) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: metal binding protein
• 由来する生物種: Aspergillus oryzae (Yellow koji mold)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27120.38

構造登録者

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. (登録日: 2014-02-05, 公開日: 2015-01-28, 最終更新日: 2025-03-26)

主引用文献

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

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: 25608804
DOI: 10.1038/ncomms6961

実験手法

X-RAY DIFFRACTION (1.5 Å)