4B5Q

The lytic polysaccharide monooxygenase GH61D structure from the basidiomycota fungus Phanerochaete chrysosporium

4B5Q の概要

• エントリーDOI: 10.2210/pdb4b5q/pdb
• 分子名称: GLYCOSIDE HYDROLASE FAMILY 61 PROTEIN D, COPPER (II) ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: hydrolase, metal binding site, cellulose degradation, copper monooxygenase
• 由来する生物種: PHANEROCHAETE CHRYSOSPORIUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47519.19

構造登録者

Wu, M.,Beckham, G.T.,Larsson, A.M.,Ishida, T.,Kim, S.,Crowley, M.F.,Payne, C.M.,Horn, S.J.,Westereng, B.,Stahlberg, J.,Eijsink, V.G.H.,Sandgren, M. (登録日: 2012-08-07, 公開日: 2013-04-03, 最終更新日: 2024-10-23)

主引用文献

Wu, M.,Beckham, G.T.,Larsson, A.M.,Ishida, T.,Kim, S.,Payne, C.M.,Himmel, M.E.,Crowley, M.F.,Horn, S.J.,Westereng, B.,Igarashi, K.,Samejima, M.,Stahlberg, J.,Eijsink, V.G.H.,Sandgren, M.
Crystal Structure and Computational Characterization of the Lytic Polysaccharide Monooxygenase Gh61D from the Basidiomycota Fungus Phanerochaete Chrysosporium
J.Biol.Chem., 288:12828-, 2013

PubMed Abstract: Carbohydrate structures are modified and degraded in the biosphere by a myriad of mostly hydrolytic enzymes. Recently, lytic polysaccharide mono-oxygenases (LPMOs) were discovered as a new class of enzymes for cleavage of recalcitrant polysaccharides that instead employ an oxidative mechanism. LPMOs employ copper as the catalytic metal and are dependent on oxygen and reducing agents for activity. LPMOs are found in many fungi and bacteria, but to date no basidiomycete LPMO has been structurally characterized. Here we present the three-dimensional crystal structure of the basidiomycete Phanerochaete chrysosporium GH61D LPMO, and, for the first time, measure the product distribution of LPMO action on a lignocellulosic substrate. The structure reveals a copper-bound active site common to LPMOs, a collection of aromatic and polar residues near the binding surface that may be responsible for regio-selectivity, and substantial differences in loop structures near the binding face compared with other LPMO structures. The activity assays indicate that this LPMO primarily produces aldonic acids. Last, molecular simulations reveal conformational changes, including the binding of several regions to the cellulose surface, leading to alignment of three tyrosine residues on the binding face of the enzyme with individual cellulose chains, similar to what has been observed for family 1 carbohydrate-binding modules. A calculated potential energy surface for surface translation indicates that P. chrysosporium GH61D exhibits energy wells whose spacing seems adapted to the spacing of cellobiose units along a cellulose chain.

PubMed: 23525113
DOI: 10.1074/JBC.M113.459396

実験手法

X-RAY DIFFRACTION (1.75 Å)