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  Nucleotide interactions of the human voltage-dependent anion channel.

Villinger, S., Giller, K., Bayrhuber, M., Lange, A., Griesinger, C., Becker, S., et al. (2014). Nucleotide interactions of the human voltage-dependent anion channel. Journal of Biological Chemistry, 289(19), 13397-13406. doi:10.1074/jbc.M113.524173.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-BBD0-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-3D6F-D
Genre: Journal Article

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 Creators:
Villinger, S.1, Author              
Giller, K.1, Author              
Bayrhuber, M., Author              
Lange, A.2, Author              
Griesinger, C.1, Author              
Becker, S.1, Author              
Zweckstetter, M.3, Author              
Affiliations:
1Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
2Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society, ou_persistent35              
3Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: ATP; Membrane Proteins; NMR; Nucleotide; Organic Anion Channels; Interactions
 Abstract: Background: Human VDAC1 mediates and controls the transport of metabolites across the outer mitochondrial membrane. Results: The N-terminal helix of hVDAC1 is involved in binding to charged forms of ATP, UTP, and GTP with an important contribution from lysine 20. Conclusion: Weak binding of ATP confers specificity for ATP transport. Significance: ATP interaction mapped at residue resolution supports metabolite selectivity of VDAC. The voltage-dependent anion channel (VDAC) mediates and gates the flux of metabolites and ions across the outer mitochondrial membrane and is a key player in cellular metabolism and apoptosis. Here we characterized the binding of nucleotides to human VDAC1 (hVDAC1) on a single-residue level using NMR spectroscopy and site-directed mutagenesis. We find that hVDAC1 possesses one major binding region for ATP, UTP, and GTP that partially overlaps with a previously determined NADH binding site. This nucleotide binding region is formed by the N-terminal -helix, the linker connecting the helix to the first -strand and adjacent barrel residues. hVDAC1 preferentially binds the charged forms of ATP, providing support for a mechanism of metabolite transport in which direct binding to the charged form exerts selectivity while at the same time permeation of the Mg2+-complexed ATP form is possible.

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Language(s): eng - English
 Dates: 2014-03-252014-05-09
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.M113.524173
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 289 (19) Sequence Number: - Start / End Page: 13397 - 13406 Identifier: -