4D7V

The structure of the catalytic domain of NcLPMO9C from the filamentous fungus Neurospora crassa

4D7V の概要

• エントリーDOI: 10.2210/pdb4d7v/pdb
• 関連するPDBエントリー: 4D7U
• 分子名称: ENDOGLUCANASE II, ZINC ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, catalytic domain, hemicellulose active, aa9
• 由来する生物種: NEUROSPORA CRASSA (STRAIN ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47739.27

構造登録者

Borisova, A.S.,Isaksen, T.,Sandgren, M.,Sorlie, M.,Eijsink, V.G.H.,Dimarogona, M. (登録日: 2014-11-27, 公開日: 2015-07-22, 最終更新日: 2024-10-16)

主引用文献

Borisova, A.S.,Isaksen, T.,Dimarogona, M.,Kognole, A.A.,Mathiesen, G.,Varnai, A.,Rohr, A.K.,Payne, C.,Sorlie, M.,Sandgren, M.,Eijsink, V.G.H.,Sorlie, M.
Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity
J.Biol.Chem., 290:22955-, 2015

PubMed Abstract: The recently discovered lytic polysaccharide monooxygenases (LPMOs) carry out oxidative cleavage of polysaccharides and are of major importance for efficient processing of biomass. NcLPMO9C from Neurospora crassa acts both on cellulose and on non-cellulose β-glucans, including cellodextrins and xyloglucan. The crystal structure of the catalytic domain of NcLPMO9C revealed an extended, highly polar substrate-binding surface well suited to interact with a variety of sugar substrates. The ability of NcLPMO9C to act on soluble substrates was exploited to study enzyme-substrate interactions. EPR studies demonstrated that the Cu(2+) center environment is altered upon substrate binding, whereas isothermal titration calorimetry studies revealed binding affinities in the low micromolar range for polymeric substrates that are due in part to the presence of a carbohydrate-binding module (CBM1). Importantly, the novel structure of NcLPMO9C enabled a comparative study, revealing that the oxidative regioselectivity of LPMO9s (C1, C4, or both) correlates with distinct structural features of the copper coordination sphere. In strictly C1-oxidizing LPMO9s, access to the solvent-facing axial coordination position is restricted by a conserved tyrosine residue, whereas access to this same position seems unrestricted in C4-oxidizing LPMO9s. LPMO9s known to produce a mixture of C1- and C4-oxidized products show an intermediate situation.

PubMed: 26178376
DOI: 10.1074/JBC.M115.660183

実験手法

X-RAY DIFFRACTION (1.9 Å)