2JK4
Structure of the human voltage-dependent anion channel
Summary for 2JK4
| Entry DOI | 10.2210/pdb2jk4/pdb |
| Descriptor | VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 1 (1 entity in total) |
| Functional Keywords | vdac, porin, membrane, apoptosis, transport, mitochondrion outer membrane, mitochondrial outer membrane, membrane protein, host-virus interaction, ion transport, transmembrane, phosphoprotein, acetylation, mitochondrion, cell membrane |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 32181.99 |
| Authors | Bayrhuber, M.,Meins, T.,Habeck, M.,Becker, S.,Giller, K.,Villinger, S.,Vonrhein, C.,Griesinger, C.,Zweckstetter, M.,Zeth, K. (deposition date: 2008-08-15, release date: 2008-10-14, Last modification date: 2024-05-08) |
| Primary citation | Bayrhuber, M.,Meins, T.,Habeck, M.,Becker, S.,Giller, K.,Villinger, S.,Vonrhein, C.,Griesinger, C.,Zweckstetter, M.,Zeth, K. Structure of the Human Voltage-Dependent Anion Channel. Proc.Natl.Acad.Sci.USA, 105:15370-, 2008 Cited by PubMed Abstract: The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitochondrially induced apoptosis. Here, we present the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography. Human VDAC1 (hVDAC1) adopts a beta-barrel architecture composed of 19 beta-strands with an alpha-helix located horizontally midway within the pore. Bioinformatic analysis indicates that this channel architecture is common to all VDAC proteins and is adopted by the general import pore TOM40 of mammals, which is also located in the MOM. PubMed: 18832158DOI: 10.1073/PNAS.0808115105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.1 Å) |
Structure validation
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