Approaching the structure of human VDAC1, a key molecule in mitochondrial cross-talk

Journal of bioenergetics - Tập 40 - Trang 127-132 - 2008
Kornelius Zeth1, Thomas Meins2, Clemens Vonrhein3
1Department of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany
2Department of Membrane Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany
3Global Phasing Ltd., Cambridge, UK

Tóm tắt

The voltage dependent anion-channel, VDAC, is the major constitutive protein of the outer membrane of mitochondria. Functionally, VDAC is involved in the exchange of small metabolites over the mitochondrial outer membrane and supports enzymes of the cytoplasm with energy precursors i.e. ATP. Moreover, the channel alone or in complex with proteins of the inner mitochondrial membrane or the intermembrane space provides a basis for docking of cytosolic proteins which can regulate outer membrane permeability in several ways. Structurally, this channel has a bacterial origin by evolution and partly resembles bacterial porin functions. However, the structure seems more complex as a variety of interactions on both channel sides can occur. Therefore, our work described is aiming to determine the structure of VDAC at atomic resolution and together with functional data to understand better how this channel can carry out such a variety of differing functions.

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