Journal:Acta Cryst D:S2059798321006628
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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 <scene name='88/886512/Cv/8'>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 <scene name='88/886512/Cv/6'>copper ion and the residues coordinating it</scene> are shown. 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. Comparison of the substrate binding sites of McAA9A and selected AA9 LPMOs, key residues lining the flat surface of: | + | 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/8'>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 <scene name='88/886512/Cv/6'>copper ion and the residues coordinating it</scene> are shown. 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. |
| - | *<scene name='88/886512/Cv2/ | + | |
| + | Comparison of the substrate binding sites of McAA9A and selected AA9 LPMOs, key residues lining the flat surface of: | ||
| + | *<scene name='88/886512/Cv2/4'>McAA9F</scene> (PDB entry [[7ntl]]). | ||
*<scene name='88/886512/Cv1/3'>TaAA9A</scene> (PDB entry [[2yet]]). | *<scene name='88/886512/Cv1/3'>TaAA9A</scene> (PDB entry [[2yet]]). | ||
*<scene name='88/886512/Cv/15'>LsAA9A</scene> (PDB entry [[5acf]]). | *<scene name='88/886512/Cv/15'>LsAA9A</scene> (PDB entry [[5acf]]). | ||
| - | *<scene name='88/886512/Cv/ | + | *<scene name='88/886512/Cv/19'>CvAA9A in complex with cellohexaose</scene> (PDB entry [[6yde]]). |
Loop regions corresponding to L2, L3, and LC for each protein are colored green, magenta, and cyan, respectively. | Loop regions corresponding to L2, L3, and LC for each protein are colored green, magenta, and cyan, respectively. | ||
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| + | <scene name='88/886512/Cv2/5'>The flat surface of McAA9F</scene>. | ||
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| + | <scene name='88/886512/Cv3/6'>Superposition of McAA9F, TaAA9A, LsAA9A, and CvAA9A</scene>. The key residues lining the flat surface are shown in ball-and-stick representation and are colored: McAA9F in salmon, TaAA9A in lemon chiffon, LsAA9A in yellow, and CvAA9A in hot pink. The other residues are shown as trace and are colored in gainsboro. | ||
The structure further contains a rare <scene name='88/886512/Cv/5'>succinimide</scene> substitution that has not been seen in other LPMOs. | The structure further contains a rare <scene name='88/886512/Cv/5'>succinimide</scene> substitution that has not been seen in other LPMOs. | ||
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| + | '''PDB reference:''' McAA9F, [[7ntl]]. | ||
<b>References</b><br> | <b>References</b><br> | ||
Current revision
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
