7S7S

Crystal structure of hydrophobin SC16, P21212

Summary for 7S7S

• Entry DOI: 10.2210/pdb7s7s/pdb
• Related: 7S86
• Descriptor: Hydrophobin (2 entities in total)
• Functional Keywords: hydrophobin, self-assembly, surface modifier, structural protein
• Biological source: Schizophyllum commune
• Total number of polymer chains: 1
• Total formula weight: 10098.56

Authors

Vergunst, K.L.,Langelaan, D.N. (deposition date: 2021-09-17, release date: 2022-01-19, Last modification date: 2024-10-23)

Primary citation

Vergunst, K.L.,Langelaan, D.N.
The N-terminal tail of the hydrophobin SC16 is not required for rodlet formation.
Sci Rep, 12:366-366, 2022

PubMed 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. Surprisingly, removal of the N-terminal tail did not influence the self-assembly kinetics of SC16 or the morphology of its rodlets. These results suggest that other regions of this hydrophobin class are required for rodlet formation and indicate that the N-terminal tail of SC16 is amenable to modification so that functionalized hydrophobin assemblies can be created.

PubMed: 35013607
DOI: 10.1038/s41598-021-04223-6

Experimental method

X-RAY DIFFRACTION (2.2 Å)