Structural Study of the Exocyst Subunit Human Sec6

In eukaryotic cells, vesicular transport plays a crucial role in the docking and fusion of secretory vesicles with their respective target membranes. This intricate process is dependent on a complex network of multiple molecules. One of the important processes is tethering. The exocyst complex facilitates the tethering of secretory vesicles to the plasma membrane during exocytosis. The Sec6 subunit in yeast interacts with other exocyst subunits and may regulate SNARE assembly, which is crucial for understanding the assembly mechanism of exocyst and its interaction with SNARE. In this study, we designed two truncated forms of HuSec6, HuSec6 121-734 and HuSec6 121-745, based on results of bioinformatics analysis. We expressed and purified the proteins in E. coli, obtaining a protein purity of over 95% and protein crystals. X-ray diffraction results showed a resolution of approximately 9 Å for the crystals, providing a solid foundation for the crystal structure analysis of HuSec6.