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The pink-colored protein from the fungus Pleurotus salmoneostramineus(PsPCP) possesses unusual primary sequences with little resemblance to those of known proteins and exhibits a red color in aqueous solution. To understand the pigmentation mechanism of PsPCP, we elucidated the X-ray crystal structure of the native PsPCP. We identified a highly conjugated polyene ligand 2-dehydro-3-deoxylaetiporic acid A as a chromophore ligand, whose solution exhibits yellow. The crystal structure of PsPCP indicated that the ligand is secured in the central cavity and anchored at both termini by hydrophilic interactions and that surrounding residues show CH-pi and C–H···O hydrogen bondings. Geometrical analyses of the bound ligand demonstrated that the conjugated C–C and C═C bonds exhibit similar bond distances. The result indicated enhanced electron delocalization within the conjugated CC bond system, resulting in a redshift of the chromophore ligand. The computational estimates of the UV-vis spectra support the view that the electron delocalization within the conjugated CC bonds system of the bound ligand, induced by the specific ligand geometry within a limited space of PsPCP cavity, is responsible for the red pigmentation of PsPCP. Thus, we propose that the coloring mechanism of PsPCP, which constrains the geometry of a highly conjugated polyene ligand, is a novel type of pigment chemistry.

Bacterial α-1,3-glucanase, classified as glycoside hydrolase (GH) family 87, has been divided into 3 subgroups based on differences in gene sequences in the catalytic domain. The enzymatic properties of subgroups 1 and 3 of several bacteria have been previously investigated and reported; however, the chemical characterization of subgroup 2 enzymes has not been previously conducted. The α-1,3-glucanase gene from Paenibacillus alginolyticusNBRC15375 (PaAgl) belonging to subgroup 2 of GH family 87 was cloned and expressed in Escherichia coli. PgAgl-N1 (subgroup 3) and PgAgl-N2 (subgroup 1) from P. glycanilyticusNBRC16188 were expressed in E. coli, and their enzymatic characteristics were compared. The amino acid sequence of PaAgl demonstrated that the homology was significantly lower in other subgroups when only the catalytic domain was compared. The oligosaccharide products of the mutan-degrading reaction seemed to have different characteristics among subgroups 1, 2, and 3 in GH family 87.Graphical AbstractPaAgl, PgAgl-N1, and PgAgl-N2 were used to elucidate the differences in properties among subgroups 1, 2, and 3 of GH family 87.