Fig. 1

Structure of T. fusca AA10A and the domain arrangement of T. fusca LPMOs. a Overall structure of TfAA10A shown as a ribbon with red α-helices, yellow β-sheets and green loops with a surface representation positioned to emphasize the planar binding surface. Position of surface mutant residues is shown as sticks in red (His37), magenta (Tyr213), blue (Asn83, both conformations), and cyan Trp82). An orange ball depicts the copper atom and to complete the active site His144 is shown as gray sticks. b Electron density figure showing the active site of T. fusca AA10A chain A. Residues are shown as sticks with gray carbons, blue nitrogens and red oxygens. The copper atom is shown as an orange ball. The 2Fo-Fc map is shown as a dark blue mesh and has been calculated at 1.2 sigma 7.5 Å around the copper atom. The Fo-Fc map is green at 3.2 sigma and has been rendered 7.5 Å from the copper atom. Both maps were calculated using REFMAC5 and MAPMASK with the CCP4 interface [19, 23]. c TfAA10A and Streptomyces coelicolor lytic polysaccharide monooxygenase superimposed. TfAA10A is shown as a green ribbon with the discussed residues labeled and shown as green sticks. Streptomyces coelicolor lytic polysaccharide monooxygenase is shown in magenta. d Domain arrangement of T. fusca LPMOs showing TfAA10A and the multiple TfAA10B domains