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Fig. 5 | BMC Biotechnology

Fig. 5

From: A novel starch-binding laccase from the wheat pathogen Zymoseptoria tritici highlights the functional diversity of ascomycete laccases

Fig. 5

Superimposition of modeled ZtrLac1A with the structures from the ascomycetes M. albomyces (MalLac1A, 1GW0), T. arenaria (TarLac1A, 3PPS), Botyris aclada (BacLac1A, 3SQR) and A. niger (AniLac1A, 5LM8). a The loop A flanking the T1 substrate binding site in ZtrLac1A (dark blue) is variable with respect to size and sequence from the structurally characterized MalLac1A (light brown), TarLac1A (red), BacLac1A (Cyan) as well as AniLac1A (green). b Superposition of C-termini of ZtrLac1A, MalLac1A, TarLac1A, BacLac1A and AniLac1A. The Cu 1 and Cu 2–3 are shown as red spheres. Structures were rendered using PYMOL v1.8 software (Schrödinger, LLC, Palo Alto, CA). The sequence alignment of these functionally relevant structural elements is shown and divergent segments and amino acid substitutions that involve large changes in chemistry or length of sidechains are highlighted in grey shades

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BMC Biotechnology

ISSN: 1472-6750

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