Skip to main content
Fig. 3 | Biotechnology for Biofuels and Bioproducts

Fig. 3

From: Structure–function characterization of two enzymes from novel subfamilies of manganese peroxidases secreted by the lignocellulose-degrading Agaricales fungi Agrocybe pediades and Cyathus striatus

Fig. 3

Mn2+-binding sites in the crystal structures of Ape-MnP1 (A), Cst-MnP1 (B) and Pch-MnP1 (C). Manganese coordination spheres (the cation shown as a pink sphere) include the internal heme propionate and: A) Asp35, Asp177, Gln333 and two water molecules (w30 and w32) in Ape-MnP1; B) Glu36, Asp176 and three water molecules (w94, w104 and w107) in Cst-MnP1; and C) Glu35, Glu39, Asp179 and two water molecules (w1040 and w1108) in the previously characterized Pch-MnP1. The green side chains superimposed in A and C correspond to the orientation of the amino acids in the structures obtained in the absence of Mn2+. Other residues previously predicted [28] to be coordinating manganese in Ape-MnP1 and Cst-MnP1 are indicated by black lettering

Back to article page

Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

Contact us