6Z5Y

Structure of a novel LPMO from Phytophthora infestans

Summary for 6Z5Y

• Entry DOI: 10.2210/pdb6z5y/pdb
• Descriptor: Lytic Polysaccharide Monooxygenase, COPPER (II) ION, TRIETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: lytic polysaccharide monooxygenase, copper, lpmo, metal binding protein
• Biological source: Phytophthora infestans (strain T30-4) (Potato late blight fungus)
• Total number of polymer chains: 2
• Total formula weight: 40310.33

Authors

Urresti, S.,Davies, G.J. (deposition date: 2020-05-27, release date: 2021-08-11, Last modification date: 2024-11-13)

Primary citation

Sabbadin, F.,Urresti, S.,Henrissat, B.,Avrova, A.O.,Welsh, L.R.J.,Lindley, P.J.,Csukai, M.,Squires, J.N.,Walton, P.H.,Davies, G.J.,Bruce, N.C.,Whisson, S.C.,McQueen-Mason, S.J.
Secreted pectin monooxygenases drive plant infection by pathogenic oomycetes.
Science, 373:774-779, 2021

PubMed Abstract: The oomycete is a damaging crop pathogen and a model organism to study plant-pathogen interactions. We report the discovery of a family of copper-dependent lytic polysaccharide monooxygenases (LPMOs) in plant pathogenic oomycetes and its role in plant infection by We show that LPMO-encoding genes are up-regulated early during infection and that the secreted enzymes oxidatively cleave the backbone of pectin, a charged polysaccharide in the plant cell wall. The crystal structure of the most abundant of these LPMOs sheds light on its ability to recognize and degrade pectin, and silencing the encoding gene in inhibits infection of potato, indicating a role in host penetration. The identification of LPMOs as virulence factors in pathogenic oomycetes opens up opportunities in crop protection and food security.

PubMed: 34385392
DOI: 10.1126/science.abj1342

Experimental method

X-RAY DIFFRACTION (1.01 Å)