5FOH

Crystal structure of the catalytic domain of NcLPMO9A

Summary for 5FOH

• Entry DOI: 10.2210/pdb5foh/pdb
• Descriptor: POLYSACCHARIDE MONOOXYGENASE, alpha-D-mannopyranose, COPPER (II) ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, aa9, lytic polysaccharide monooxygenase
• Biological source: NEUROSPORA CRASSA
• Total number of polymer chains: 1
• Total formula weight: 24099.07

Authors

Westereng, B.,Kracun, S.K.,Dimarogona, M.,Mathiesen, G.,Willats, W.G.T.,Sandgren, M.,Aachmann, F.L.,Eijsink, V.G.H. (deposition date: 2015-11-18, release date: 2016-12-07, Last modification date: 2024-10-23)

Primary citation

Petrovic, D.M.,Varnai, A.,Dimarogona, M.,Mathiesen, G.,Sandgren, M.,Westereng, B.,Eijsink, V.G.H.
Comparison of three seemingly similar lytic polysaccharide monooxygenases fromNeurospora crassasuggests different roles in plant biomass degradation.
J.Biol.Chem., 2019

PubMed Abstract: Many fungi produce multiple lytic polysaccharide monooxygenases (LPMOs) with seemingly similar functions, but the biological reason for this multiplicity remains unknown. To address this question, here we carried out comparative structural and functional characterizations of three cellulose-active C4-oxidizing family AA9 LPMOs from the fungus , LPMO9A (NCU02240), LPMO9C (NCU02916), and LPMO9D (NCU01050). We solved the three-dimensional structure of copper-bound LPMO9A at 1.6-Å resolution and found that LPMO9A and LPMO9C, containing a CBM1 carbohydrate-binding module, bind cellulose more strongly and were less susceptible to inactivation than LPMO9D, which lacks a CBM. All three LPMOs were active on tamarind xyloglucan and konjac glucomannan, generating similar products but clearly differing in activity levels. Importantly, in some cases, the addition of phosphoric acid-swollen cellulose (PASC) had a major effect on activity: LPMO9A was active on xyloglucan only in the presence of PASC, and PASC enhanced LPMO9D activity on glucomannan. Interestingly, the three enzymes also exhibited large differences in their interactions with enzymatic electron donors, which could reflect that they are optimized to act with different reducing partners. All three enzymes efficiently used HO as a cosubstrate, yielding product profiles identical to those obtained in O-driven reactions with PASC, xyloglucan, or glucomannan. Our results indicate that seemingly similar LPMOs act preferentially on different types of copolymeric substructures in the plant cell wall, possibly because these LPMOs are functionally adapted to distinct niches differing in the types of available reductants.

PubMed: 31431506
DOI: 10.1074/jbc.RA119.008196

Experimental method

X-RAY DIFFRACTION (1.6 Å)