2K4T
Solution structure of human VDAC-1 in LDAO micelles
Summary for 2K4T
| Entry DOI | 10.2210/pdb2k4t/pdb |
| NMR Information | BMRB: 16381 |
| Descriptor | Voltage-dependent anion-selective channel protein 1 (1 entity in total) |
| Functional Keywords | membrane protein, acetylation, apoptosis, host-virus interaction, ion transport, membrane, mitochondrion, outer membrane, phosphoprotein, porin, transmembrane, transport protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Mitochondrion outer membrane: P21796 |
| Total number of polymer chains | 1 |
| Total formula weight | 31878.66 |
| Authors | Hiller, S.,Garces, R.G.,Malia, T.J.,Orekhov, V.Y.,Colombini, M.,Wagner, G. (deposition date: 2008-06-17, release date: 2008-09-09, Last modification date: 2024-05-29) |
| Primary citation | Hiller, S.,Garces, R.G.,Malia, T.J.,Orekhov, V.Y.,Colombini, M.,Wagner, G. Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science, 321:1206-1210, 2008 Cited by PubMed Abstract: The voltage-dependent anion channel (VDAC) mediates trafficking of small molecules and ions across the eukaryotic outer mitochondrial membrane. VDAC also interacts with antiapoptotic proteins from the Bcl-2 family, and this interaction inhibits release of apoptogenic proteins from the mitochondrion. We present the nuclear magnetic resonance (NMR) solution structure of recombinant human VDAC-1 reconstituted in detergent micelles. It forms a 19-stranded beta barrel with the first and last strand parallel. The hydrophobic outside perimeter of the barrel is covered by detergent molecules in a beltlike fashion. In the presence of cholesterol, recombinant VDAC-1 can form voltage-gated channels in phospholipid bilayers similar to those of the native protein. NMR measurements revealed the binding sites of VDAC-1 for the Bcl-2 protein Bcl-x(L), for reduced beta-nicotinamide adenine dinucleotide, and for cholesterol. Bcl-x(L) interacts with the VDAC barrel laterally at strands 17 and 18. PubMed: 18755977DOI: 10.1126/science.1161302 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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