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Research Article Open Access
HYD1 is a small secreted fungal protein that belongs to class I hydrophobins of G. moniliformis. It is able to spontaneously self-assemble at hydrophilic: hydrophobic interfaces into a 10 nm amphipathic rodlet monolayer. Based on this unique property, HYD1 is involved in signaling and attachment of aerial structures (like mycelia, hyphae, and spores) to hydrophobic surfaces of host plant during fungal pathogenesis. This paper seeks to construct a 3D structure of HYD1 based on multiple templates using the novel algorithm available on the M4T online server. PROCHECK, ProSA, Verify3D and 3dss server are used to analyze the quality and consistency of the generated model. The M4T_HYD1 model thus had a compatible DOPE score value of -5547.2 and showed 93.0% amino acid residues under the most favored region [A, B, L]. Evaluation of the 3D model and two templates (2f26C and 2pl6A) with ProSA revealed a compatible Z score value of -3.43, -4.31, and -4.10 respectively, indicating a comparable surface energy affinity of M4T_HDY1 with the templates. A low RMSD value between the target and the template structures upon superimposition reflects high structural connection. Hence, the predicted model proved to be well ratified in terms of geometry and energy contours, indicating that the model is reasonable and reliable for future molecular docking studies.
HYD1, Hydrophobins, Self-assemble, Amphipathic, M4T algorithm, DOPE, Superimposition, Method Validation