6YJI
Structure of FgCelDH7C
Summary for 6YJI
| Entry DOI | 10.2210/pdb6yji/pdb |
| Descriptor | FAD-binding PCMH-type domain-containing protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, FLAVIN-ADENINE DINUCLEOTIDE, ... (10 entities in total) |
| Functional Keywords | fad, linking, oxidoreductase |
| Biological source | Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) |
| Total number of polymer chains | 2 |
| Total formula weight | 111090.99 |
| Authors | Haddad Momeni, M.,Fredslund, F.,Berrin, J.G.,Abou Hachem, M.,Welner, D.H. (deposition date: 2020-04-03, release date: 2021-03-03, Last modification date: 2024-01-24) |
| Primary citation | Haddad Momeni, M.,Fredslund, F.,Bissaro, B.,Raji, O.,Vuong, T.V.,Meier, S.,Nielsen, T.S.,Lombard, V.,Guigliarelli, B.,Biaso, F.,Haon, M.,Grisel, S.,Henrissat, B.,Welner, D.H.,Master, E.R.,Berrin, J.G.,Abou Hachem, M. Discovery of fungal oligosaccharide-oxidising flavo-enzymes with previously unknown substrates, redox-activity profiles and interplay with LPMOs. Nat Commun, 12:2132-2132, 2021 Cited by PubMed Abstract: Oxidative plant cell-wall processing enzymes are of great importance in biology and biotechnology. Yet, our insight into the functional interplay amongst such oxidative enzymes remains limited. Here, a phylogenetic analysis of the auxiliary activity 7 family (AA7), currently harbouring oligosaccharide flavo-oxidases, reveals a striking abundance of AA7-genes in phytopathogenic fungi and Oomycetes. Expression of five fungal enzymes, including three from unexplored clades, expands the AA7-substrate range and unveils a cellooligosaccharide dehydrogenase activity, previously unknown within AA7. Sequence and structural analyses identify unique signatures distinguishing the strict dehydrogenase clade from canonical AA7 oxidases. The discovered dehydrogenase directly is able to transfer electrons to an AA9 lytic polysaccharide monooxygenase (LPMO) and fuel cellulose degradation by LPMOs without exogenous reductants. The expansion of redox-profiles and substrate range highlights the functional diversity within AA7 and sets the stage for harnessing AA7 dehydrogenases to fine-tune LPMO activity in biotechnological conversion of plant feedstocks. PubMed: 33837197DOI: 10.1038/s41467-021-22372-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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