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Fig. 5 | Biotechnology for Biofuels

Fig. 5

From: Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum

Fig. 5

Alignment of the GH7 TreCel7A, ThaCel7A, and TatCel7A protein sequences. Secondary structural elements of the TreCel7A structure are indicated above the alignment (β-strand arrows and α-helices) based on the 3D structure of the catalytic domain (1CEL). Strictly identical residues are marked in white letters on a black background. Regions of conserved, highly similar residues are framed in thin-lined boxes with bold letters. The figure was prepared using the ESPript web server with default parameters (http://espript.ibcp.fr; [82]). Red frames indicate loop regions of interest, with loop nomenclature underneath. The regions highlighted in blue denote N-glycosylation motifs; the colored triangles indicate the N-glycosylated asparagine residues observed in structures, where gray triangles correspond to TreCel7A, green triangles to ThaCel7A, and the blue triangle to TatCel7A. Sections of interest defined by RCA (reverse conservation analysis) are marked with blue lines and corresponding identifiers (I–IV), and residues with high S scores are marked in yellow

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