4MIF

Pyranose 2-oxidase from Phanerochaete chrysosporium, wild type from natural source

Summary for 4MIF

• Entry DOI: 10.2210/pdb4mif/pdb
• Related: 4MIG 4MIH
• Descriptor: Pyranose 2-oxidase, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: gmc oxidoreductase, rossmann fold, phbh fold, pyranose 2-oxidase, sugar oxidoreductase, flavinylation, hyphae, oxidoreductase
• Biological source: Phanerochaete chrysosporium (White-rot fungus)
• Cellular location: Periplasm : Q6QWR1
• Total number of polymer chains: 4
• Total formula weight: 280472.16

Authors

Hassan, N.,Tan, T.C.,Spadiut, O.,Pisanelli, I.,Fusco, L.,Haltrich, D.,Peterbauer, C.,Divne, C. (deposition date: 2013-08-31, release date: 2013-12-11, Last modification date: 2024-11-20)

Primary citation

Hassan, N.,Tan, T.C.,Spadiut, O.,Pisanelli, I.,Fusco, L.,Haltrich, D.,Peterbauer, C.K.,Divne, C.
Crystal structures of Phanerochaete chrysosporium pyranose 2-oxidase suggest that the N-terminus acts as a propeptide that assists in homotetramer assembly.
FEBS Open Bio, 3:496-504, 2013

PubMed Abstract: The flavin-dependent homotetrameric enzyme pyranose 2-oxidase (P2O) is found mostly, but not exclusively, in lignocellulose-degrading fungi where it catalyzes the oxidation of β-d-glucose to the corresponding 2-keto sugar concomitantly with hydrogen peroxide formation during lignin solubilization. Here, we present crystal structures of P2O from the efficient lignocellulolytic basidiomycete Phanerochaete chrysosporium. Structures were determined of wild-type PcP2O from the natural fungal source, and two variants of recombinant full-length PcP2O, both in complex with the slow substrate 3-deoxy-3-fluoro-β-d-glucose. The active sites in PcP2O and P2O from Trametes multicolor (TmP2O) are highly conserved with identical substrate binding. Our structural analysis suggests that the 17 °C higher melting temperature of PcP2O compared to TmP2O is due to an increased number of intersubunit salt bridges. The structure of recombinant PcP2O expressed with its natural N-terminal sequence, including a proposed propeptide segment, reveals that the first five residues of the propeptide intercalate at the interface between A and B subunits to form stabilizing, mainly hydrophobic, interactions. In the structure of mature PcP2O purified from the natural source, the propeptide segment in subunit A has been replaced by a nearby loop in the B subunit. We propose that the propeptide in subunit A stabilizes the A/B interface of essential dimers in the homotetramer and that, upon maturation, it is replaced by the loop in the B subunit to form the mature subunit interface. This would imply that the propeptide segment of PcP2O acts as an intramolecular chaperone for oligomerization at the A/B interface of the essential dimer.

PubMed: 24282677
DOI: 10.1016/j.fob.2013.10.010

Experimental method

X-RAY DIFFRACTION (1.8 Å)