The N-terminal tail of the hydrophobin SC16 is not required for rodlet formation.

ABSTRACT: Hydrophobins are small proteins that are secreted by fungi, accumulate at interfaces, modify surface hydrophobicity, and self-assemble into large amyloid-like structures. These unusual properties make hydrophobins an attractive target for commercial applications as green emulsifiers and surface modifying agents. Hydrophobins have diverse sequences and tertiary structures, and depending on the hydrophobin, different regions of their structure have been proposed to be required for self-assembly. To provide insight into the assembly process, we determined the first crystal structure of a class I hydrophobin, SC16. Based on the crystal structure, we identified a putative intermolecular contact that may be important for rodlet assembly and was formed in part by the N-terminal tail of SC16. Surp

SUBMITTER: Vergunst KL 

PROVIDER: S-EPMC8748815 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature