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2k4t
From Proteopedia
| 2k4t, 20 NMR models () | |||||||||
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| Gene: | VDAC1, VDAC (Homo sapiens) | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Solution structure of human VDAC-1 in LDAO micelles
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.
Solution structure of the integral human membrane protein VDAC-1 in detergent micelles., Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G, Science. 2008 Aug 29;321(5893):1206-10. PMID:18755977
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2K4T is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G. Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science. 2008 Aug 29;321(5893):1206-10. PMID:18755977 doi:321/5893/1206
Page seeded by OCA on Wed Feb 18 09:53:59 2009
Categories: Homo sapiens | Colombini, M. | Garces, R G. | Hiller, S. | Malia, T J. | Orekhov, V Y. | Wagner, G. | Acetylation | Apoptosis | Host-virus interaction | Ion transport | Membrane | Membrane protein | Mitochondrion | Outer membrane | Phosphoprotein | Porin | Transmembrane | Transport protein
