Crystal packing analysis of murine VDAC1 crystals in a lipidic environment reveals novel insights on oligomerization and orientation.

ABSTRACT: All eukaryotic cells require efficient trafficking of metabolites between the mitochondria and the rest of the cell. This exchange is carried out by the dominant protein in the outer mitochondrial membrane (OMM), the Voltage Dependent Anion Channel (VDAC), which serves as the primary pathway for the exchange of ions and metabolites between the cytoplasm and the intermembrane space of the mitochondria. Additionally, VDAC provides a scaffold for the binding of modulator proteins to the mitochondria and has been implicated in mitochondria-dependent cell death. We recently determined the structure of the murine VDAC1 (mVDAC1) at 2.3 A resolution crystallized in a native-like bilayer environment. The high-resolution structure provided concise structural details about the voltage-sensing N-termi

SUBMITTER: Ujwal R 

PROVIDER: S-EPMC3719987 | biostudies-literature | 2009 May-Jun

REPOSITORIES: biostudies-literature