7ZE9

Structure of an AA16 LPMO-like protein

これはPDB形式変換不可エントリーです。

7ZE9 の概要

• エントリーDOI: 10.2210/pdb7ze9/pdb
• 分子名称: Chitin-binding type-4 domain-containing protein, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: carbohydrate active enzyme, auxillary activity, lpmo, aa16, metal binding protein
• 由来する生物種: Thermothelomyces thermophilus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 65826.98

構造登録者

Huang, Z.,Banerjee, S.,Muderspach, S.J.,Sun, P.,van Berkel, W.J.H.,Kabel, M.A.,Lo Leggio, L. (登録日: 2022-03-30, 公開日: 2023-03-15, 最終更新日: 2024-05-01)

主引用文献

Sun, P.,Huang, Z.,Banerjee, S.,Kadowaki, M.A.S.,Veersma, R.J.,Magri, S.,Hilgers, R.,Muderspach, S.J.,Laurent, C.V.F.P.,Ludwig, R.,Cannella, D.,Lo Leggio, L.,van Berkel, W.J.H.,Kabel, M.A.
AA16 Oxidoreductases Boost Cellulose-Active AA9 Lytic Polysaccharide Monooxygenases from Myceliophthora thermophila.
Acs Catalysis, 13:4454-4467, 2023

PubMed Abstract: Copper-dependent lytic polysaccharide monooxygenases (LPMOs) classified in Auxiliary Activity (AA) families are considered indispensable as synergistic partners for cellulolytic enzymes to saccharify recalcitrant lignocellulosic plant biomass. In this study, we characterized two fungal oxidoreductases from the new AA16 family. We found that AA16A from and AA16A from did not catalyze the oxidative cleavage of oligo- and polysaccharides. Indeed, the AA16A crystal structure showed a fairly LPMO-typical histidine brace active site, but the cellulose-acting LPMO-typical flat aromatic surface parallel to the histidine brace region was lacking. Further, we showed that both AA16 proteins are able to oxidize low-molecular-weight reductants to produce HO. The oxidase activity of the AA16s substantially boosted cellulose degradation by four AA9 LPMOs from (LPMO9s) but not by three AA9 LPMOs from (LPMO9s). The interplay with LPMO9s is explained by the HO-producing capability of the AA16s, which, in the presence of cellulose, allows the LPMO9s to optimally drive their peroxygenase activity. Replacement of AA16A by glucose oxidase (GOX) with the same HO-producing activity could only achieve less than 50% of the boosting effect achieved by AA16A, and earlier LPMO9B inactivation (6 h) was observed. To explain these results, we hypothesized that the delivery of AA16-produced HO to the LPMO9s is facilitated by protein-protein interaction. Our findings provide new insights into the functions of copper-dependent enzymes and contribute to a further understanding of the interplay of oxidative enzymes within fungal systems to degrade lignocellulose.

PubMed: 37066045
DOI: 10.1021/acscatal.3c00874

実験手法

X-RAY DIFFRACTION (2.646 Å)