Journal Article

DZNE-2020-03702

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Nucleotide interactions of the human voltage-dependent anion channel.

Villinger, S. ; Giller, K. ; Bayrhuber, M. ; Lange, A. ; Griesinger, C. ; Becker, S. ; Zweckstetter, M. (Last author)DZNE*

2014
Soc.60645 Bethesda, Md.

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Please use a persistent id in citations: doi:10.1074/jbc.M113.524173

Abstract: 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 α-helix, the linker connecting the helix to the first β-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 Mg(2+)-complexed ATP form is possible.

Keyword(s): Adenosine Triphosphate: chemistry (MeSH) ; Adenosine Triphosphate: genetics (MeSH) ; Adenosine Triphosphate: metabolism (MeSH) ; Biological Transport, Active: physiology (MeSH) ; Guanosine Triphosphate: chemistry (MeSH) ; Guanosine Triphosphate: genetics (MeSH) ; Guanosine Triphosphate: metabolism (MeSH) ; Humans (MeSH) ; NAD: chemistry (MeSH) ; NAD: genetics (MeSH) ; NAD: metabolism (MeSH) ; Protein Binding (MeSH) ; Protein Structure, Secondary (MeSH) ; Uridine Triphosphate: chemistry (MeSH) ; Uridine Triphosphate: genetics (MeSH) ; Uridine Triphosphate: metabolism (MeSH) ; Voltage-Dependent Anion Channel 1: chemistry (MeSH) ; Voltage-Dependent Anion Channel 1: genetics (MeSH) ; Voltage-Dependent Anion Channel 1: metabolism (MeSH) ; VDAC1 protein, human ; NAD ; Guanosine Triphosphate ; Adenosine Triphosphate ; Voltage-Dependent Anion Channel 1 ; Uridine Triphosphate

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Contributing Institute(s):

1. Structural Biology in Dementia (AG Zweckstetter)

Research Program(s):

1. 342 - Disease Mechanisms and Model Systems (POF3-342) (POF3-342)

Appears in the scientific report 2014

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Database coverage:
; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; PubMed Central ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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