Crystal structural characterization reveals novel oligomeric interactions of human voltage-dependent anion channel 1.

ABSTRACT: Voltage-dependent anion channel 1 (VDAC1), which is located in the outer mitochondrial membrane, plays important roles in various cellular processes. For example, oligomerization of VDAC1 is involved in the release of cytochrome c to the cytoplasm, leading to apoptosis. However, it is unknown how VDAC1 oligomerization occurs in the membrane. In the present study, we determined high-resolution crystal structures of oligomeric human VDAC1 (hVDAC1) prepared by using an Escherichia coli cell-free protein synthesis system, which avoided the need for denaturation and refolding of the protein. Broad-range screening using a bicelle crystallization method produced crystals in space groups C222 and P22₁ 2₁ , which diffracted to a resolution of 3.10 and 3.15 Å, respectively. Eac

SUBMITTER: Hosaka T 

PROVIDER: S-EPMC5563135 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature