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6IBJ

Copper binding protein from Laetisaria arvalis (LaX325)

Summary for 6IBJ
Entry DOI10.2210/pdb6ibj/pdb
Related6IBH 6IBI
DescriptorAuxiliary activity CAZyme, 2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (4 entities in total)
Functional Keywordsauxiliary activity cazyme, metal binding protein
Biological sourceLaetisaria arvalis
Total number of polymer chains1
Total formula weight17612.40
Authors
Frandsen, K.E.H.,Tandrup, T.,Labourel, A.,Haon, M.,Berrin, J.-G.,Lo Leggio, L. (deposition date: 2018-11-30, release date: 2019-11-13, Last modification date: 2024-10-16)
Primary citationLabourel, A.,Frandsen, K.E.H.,Zhang, F.,Brouilly, N.,Grisel, S.,Haon, M.,Ciano, L.,Ropartz, D.,Fanuel, M.,Martin, F.,Navarro, D.,Rosso, M.N.,Tandrup, T.,Bissaro, B.,Johansen, K.S.,Zerva, A.,Walton, P.H.,Henrissat, B.,Leggio, L.L.,Berrin, J.G.
A fungal family of lytic polysaccharide monooxygenase-like copper proteins.
Nat.Chem.Biol., 16:345-350, 2020
Cited by
PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that play a key role in the oxidative degradation of various biopolymers such as cellulose and chitin. While hunting for new LPMOs, we identified a new family of proteins, defined here as X325, in various fungal lineages. The three-dimensional structure of X325 revealed an overall LPMO fold and a His brace with an additional Asp ligand to Cu(II). Although LPMO-type activity of X325 members was initially expected, we demonstrated that X325 members do not perform oxidative cleavage of polysaccharides, establishing that X325s are not LPMOs. Investigations of the biological role of X325 in the ectomycorrhizal fungus Laccaria bicolor revealed exposure of the X325 protein at the interface between fungal hyphae and tree rootlet cells. Our results provide insights into a family of copper-containing proteins, which is widespread in the fungal kingdom and is evolutionarily related to LPMOs, but has diverged to biological functions other than polysaccharide degradation.
PubMed: 31932718
DOI: 10.1038/s41589-019-0438-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

226707

건을2024-10-30부터공개중

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