9FDL

Crystal structure of the catalytic domain of an AA9 lytic polysaccharide monooxygenase from Thermothelomyces thermophilus (TtLPMO9F)

Summary for 9FDL

• Entry DOI: 10.2210/pdb9fdl/pdb
• Descriptor: Glycoside hydrolase family 61 protein, DI(HYDROXYETHYL)ETHER, TETRAETHYLENE GLYCOL, ... (7 entities in total)
• Functional Keywords: lpmo, aa9, metal binding protein
• Biological source: Thermothelomyces thermophilus ATCC 42464
• Total number of polymer chains: 3
• Total formula weight: 73048.60

Authors

Kosinas, C.,Dimarogona, M.,Topakas, E. (deposition date: 2024-05-17, release date: 2024-12-25)

Primary citation

Kosinas, C.,Chorozian, K.,Sandgren, M.,Topakas, E.,Dimarogona, M.
Mutational study of a lytic polysaccharide monooxygenase from Myceliophthora thermophila (MtLPMO9F): Structural insights into substrate specificity and regioselectivity.
Int.J.Biol.Macromol., 288:138574-138574, 2024

PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are key enzymes for the biotechnological exploitation of lignocellulosic biomass, yet their efficient application depends on the in-depth understanding of their mechanism of action. Here, we describe the structural and mutational characterization of a C4-active LPMO from Myceliophthora thermophila, MtLPMO9F, that belongs to auxiliary activity family 9 (AA9). MtLPMO9F is active on cellulose, cello-oligosaccharides and xyloglucan. The crystal structure of MtLPMO9F catalytic domain, determined at 2.3 Å resolution, revealed a double conformation for loop L3 with a potential implication in the formation of aglycon subsites. Product analysis of reactions with cello-oligosaccharides showed a prevalent -4 to +2 binding mode. Subsequent biochemical characterization of 4 MtLPMO9F point mutants further provided insights in LPMO structure-function relationships regarding both substrate binding and the role of second-coordination sphere residues.

PubMed: 39662565
DOI: 10.1016/j.ijbiomac.2024.138574

Experimental method

X-RAY DIFFRACTION (2.33 Å)