English
Structural Differentiation of Membrane-Associated and Cytosolic Glycosyltransferases: An AlphaFold3-Based Comparative Structural Analysis of GT2 and GT3 in Trichoderma harzianum
Dong-Ryeol Yu1, Yu-Bin Park1, Yoon-Seo Jang1, Tae-Seok Oh1,
Youn-Jin Park2, Myoung-Jun Jang1,3*
1Department of Plant Resources, Kongju National University,
2Kongju National University Legumes Green Manure Resource Center
3Center for Smart Future Agricultural Education and Research, College of Industrial Sciences, Kongju National University
*Email: plant119@kongju.ac.kr
This study analyzed the structural characteristics and potential functional differentiation This study analyzed the structural characteristics and potential functional differentiation of GT2 and GT3 in Trichoderma harzianum. Using RNA-seq-based sequence information, protein topology was predicted, three-dimensional structures were modeled with AlphaFold3, and model quality was evaluated using pLDDT, PAE, and Ramachandran plots. GT2 was predicted to be a plasma membrane-associated protein with four transmembrane helices, whereas GT3 was predicted to be a cytosolic protein lacking both a signal peptide and transmembrane helices. Structurally, GT2 and GT3 were classified as GT-A and GT-B fold proteins, respectively, confirming that the two proteins adopt distinct folding architectures. In addition, the predicted structures of both proteins showed relatively high confidence in their core domains, and conserved motifs were associated with the formation of pocket walls or the interdomain cleft around the α/β core, suggesting their possible roles in stabilizing pocket architecture and mediating acceptor recognition. These results indicate that GT2 and GT3 are structurally differentiated glycosyltransferases in T. harzianum and provide a structural basis for interpreting their cell wall-related functions.
