Journal:Acta Cryst D:S2059798321006628
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | The thermophilic fungus ''Malbranchea cinnamomea'' encodes eight lytic polysaccharide monooxygenases (LPMOs) from the Auxiliary Activities family 9 (AA9), four of which have been shown to oxidatively cleave various polysaccharides. Here we solved the structure of McAA9F, which is a C1/C4-oxidizing LPMO able to cleave both crystalline and soluble glycans. The structure reveals that McAA9F has an overall similar fold as other solved AA9 enzymes, but also has different loop structures than what have previously been linked to activity on soluble oligosaccharides. The structure further contains a rare succinimide substitution that has not been seen in other LPMOs. | + | The thermophilic fungus ''Malbranchea cinnamomea'' encodes eight lytic polysaccharide monooxygenases (LPMOs) from the Auxiliary Activities family 9 (AA9), four of which have been shown to oxidatively cleave various polysaccharides. Here we solved the <scene name='88/886512/Cv/4'>structure of McAA9F</scene>, which is a C1/C4-oxidizing LPMO able to cleave both crystalline and soluble glycans. The structure is colored from N- to C-terminus, blue to red. The copper ion and the residues coordinating it are shown. The position of the succinimide found in place of Asp10 in the loop between strands β1 and β2 is identified by a white arrow and the loops forming the flat surface comprising the substrate binding face are labelled (L2, L3, L8, LS, LC). The structure reveals that McAA9F has an overall similar fold as other solved AA9 enzymes, but also has different loop structures than what have previously been linked to activity on soluble oligosaccharides. The structure further contains a rare succinimide substitution that has not been seen in other LPMOs. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 07:54, 6 July 2021
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