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Fig. 2 | Biotechnology for Biofuels

Fig. 2

From: Lytic polysaccharide monooxygenases from Myceliophthora thermophila C1 differ in substrate preference and reducing agent specificity

Fig. 2

Structure-based sequence alignment of MtLPMO9A, MtLPMO9B and MtLPMO9C. The structure-based sequence alignments of MtLPMO9A, MtLPMO9B and MtLPMO9C were made using three known sequences of a C1-(PcLPMO9D; PDB ID code 4B5Q), C4-(NcLPMO9C; PDB ID code 4D7U) and C1- and C4-(TaLPMO9A; PDB ID code 3ZUD) oxidizing LPMO based on Borisova et al. [10, 14, 24, 25]. The β-strands (black arrow) and α-helices (black helix) are based on NcLPMO9C and shown above the columns [25]. The bold colored lines below the columns highlight the amino acids of the four loop regions L2 (blue), L3 (yellow), Ls (red) and LC (purple), which are involved in shaping the substrate-binding site. The highly conserved amino acid residues are presented as white letters on a red background. Amino acid residues that have comparable chemical and physical properties are presented as red letters within blue frames. Sequences are presented without the signal sequence and start from the N-terminal histidine (His1). The structure-based sequence alignment was obtained using ESPript [48]

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