PDBsum entry 6ibh

Metal binding protein

PDB id: 6ibh

Contents

Protein chains

150 a.a.

Ligands

NAG ×11

IMD

Metals

_CU ×2

Waters ×187

PDB id:

6ibh

Name:

Metal binding protein

Title:

Copper binding protein from laetisaria arvalis (lax325)

Structure:

Auxiliary activity cazyme. Chain: a, b. Engineered: yes

Source:

Laetisaria arvalis. Organism_taxid: 228946. Expressed in: komagataella pastoris. Expression_system_taxid: 4922.

Resolution:

1.82Å R-factor: 0.169 R-free: 0.208

Authors:

K.E.H.Frandsen,T.Tandrup,A.Labourel,M.Haon,J.-G.Berrin,L.Lo Leggio

Key ref:

A.Labourel et al. (2020). A fungal family of lytic polysaccharide monooxygenase-like copper proteins. Nat Chem Biol, 16, 345-350. PubMed id: 31932718 DOI: 10.1038/s41589-019-0438-8

Date:

30-Nov-18 Release date: 13-Nov-19

Protein chains

A0A4P9I8G4  (X325_WAIAR) -  Lytic polysaccharide monooxygenase-like protein X325 from Waitea arvalis

Seq: 238 a.a.

Struc: 150 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1038/s41589-019-0438-8

Nat Chem Biol 16:345-350 (2020)

PubMed id: 31932718

A fungal family of lytic polysaccharide monooxygenase-like copper proteins.

A.Labourel, K.E.H.Frandsen, F.Zhang, N.Brouilly, S.Grisel, M.Haon, L.Ciano, D.Ropartz, M.Fanuel, F.Martin, D.Navarro, M.N.Rosso, T.Tandrup, B.Bissaro, K.S.Johansen, A.Zerva, P.H.Walton, B.Henrissat, L.L.Leggio, J.G.Berrin.

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.