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Crystal structure of PQQ doamin of Pyranose Dehydrogenase from Coprinopsis cinerea: apo-from
Structural highlights
FunctionAA12_COPC7 Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars including L-galactose, L-gulose, D-talose, D-arabinose, D-lyxose, L-fucose and D-glucosone (PubMed:25121592, PubMed:25679509, PubMed:27338639). Shows significant activity toward the reverse-chair conformation of pyranoses (PubMed:25679509). Shows little or no activity toward abundant sugars such as D-glucose, D-fructose, cellobiose, as well L-xylose and L-glucose (PubMed:25121592, PubMed:25679509). This enzyme is able to direct electrical communication with electrodes, without artificial electron mediators, thus allowing direct electron transfer (DET)-type bioelectrocatalysis (PubMed:27338639). Exhibits binding affinity for insoluble cellulose (PubMed:25679509). PDH does not oxidize cello-oligosaccharides but is able to activate the C-1-oxidizing Neurospora crassa LPMO9F and the C-4-oxidizing Neurospora crassa LPMO9C thanks to the electron-tranfer activity of the cytochrome domain and the localization of PDH in the vicinity of the LPMO substrates by the CBM1 domain (PubMed:29602785).[1] [2] [3] [4] Publication Abstract from PubMedPyrroloquinoline quinone (PQQ) was discovered as a redox cofactor of prokaryotic glucose dehydrogenases in the 1960s, and subsequent studies have demonstrated its importance not only in bacterial systems but also in higher organisms. We have previously reported a novel eukaryotic quinohemoprotein that exhibited PQQ-dependent catalytic activity in a eukaryote. The enzyme, pyranose dehydrogenase, from the filamentous fungus Coprinopsis cinerea (CcPDH) of the Basidiomycete division, is composed of a catalytic PQQ-dependent domain classified as a member of the novel auxiliary activity family 12 (AA12), an AA8 cytochrome b domain, and a family 1 carbohydrate-binding module (CBM1), as defined by the Carbohydrate-Active enZymes (CAZy) database. Here, we present crystal structures of the AA12 domain in its apo and holo forms and the AA8 domain of this enzyme. The crystal structures of the holo-AA12 domain bound to PQQ provide direct evidence that eukaryotes have PQQ-dependent enzymes. The AA12 domain exhibits a six-bladed beta-propeller fold that is also present in other known PQQ-dependent glucose dehydrogenases in bacteria. A loop structure around the active site and a calcium ion binding site are unique among the known structures of bacterial quinoproteins. The AA8 cytochrome domain has a positively charged area on its molecular surface, which is partly due to the propionate group of the heme interacting with Arg181; this feature differs from that of cytochrome b in the AA8 domain of the fungal cellobiose dehydrogenase and suggests that this difference may affect the pH dependence of electron transfer.Importance Pyrroloquinoline quinone (PQQ) is known as the "third coenzyme" following nicotinamide adenine dinucleotide (NAD(+)) and flavin adenine dinucleotide (FAD). PQQ-dependent enzymes have been previously found only in prokaryotes, and the existence of a eukaryotic PQQ-dependent enzyme was in doubt. In 2014, we found an enzyme in mushrooms that catalyzes the oxidation of various sugars in a PQQ-dependent manner, which was a PQQ-dependent enzyme found in eukaryotes. This paper presents the X-ray crystal structures of this eukaryotic PQQ-dependent quinohemoprotein, which show the active site and identifies the amino acid residues involved in binding of the cofactor PQQ. The presented X-ray structures reveal that AA12 domain is in a binary complex with the coenzyme, clearly proving that PQQ-dependent enzymes exist in eukaryotes as well as prokaryotes. Because no biosynthetic system for PQQ has been reported in eukaryotes, future research on the symbiotic systems is expected. The Crystal Structure of the Catalytic Domain and the Cytochrome b Domain in a Eukaryotic PQQ-Dependent Dehydrogenase.,Takeda K, Ishida T, Yoshida M, Samejima M, Ohno H, Igarashi K, Nakamura N Appl Environ Microbiol. 2019 Oct 11. pii: AEM.01692-19. doi:, 10.1128/AEM.01692-19. PMID:31604769[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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