4MIG

Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant wild type

4MIG の概要

• エントリーDOI: 10.2210/pdb4mig/pdb
• 関連するPDBエントリー: 4MIF 4MIH
• 分子名称: Pyranose 2-oxidase, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE, 3-deoxy-3-fluoro-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: homotetramer, gmc oxidoreductase, rossmann fold, phbh fold, pyranose 2-oxidase, sugar oxidoreductase, flavinylation, hyphae, oxidoreductase
• 由来する生物種: Phanerochaete chrysosporium (White-rot fungus)
• 細胞内の位置: Periplasm : Q6QWR1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 293477.39

構造登録者

Hassan, N.,Tan, T.C.,Spadiut, O.,Pisanelli, I.,Fusco, L.,Haltrich, D.,Peterbauer, C.,Divne, C. (登録日: 2013-08-31, 公開日: 2013-12-11, 最終更新日: 2024-10-16)

主引用文献

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 In the structure of mature PcP2O purified from the natural source, the propeptide segment in subunit A has been replaced by a nearby loop in the B subunit.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

実験手法

X-RAY DIFFRACTION (1.8 Å)