4C69

ATP binding to murine voltage-dependent anion channel 1 (mVDAC1).

Summary for 4C69

• Entry DOI: 10.2210/pdb4c69/pdb
• Descriptor: VOLTAGE-DEPENDENT ANION-SELECTIVE CHANNEL PROTEIN 1, LAURYL DIMETHYLAMINE-N-OXIDE, 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE, ... (5 entities in total)
• Functional Keywords: transport protein, bicelle, outer membrane protein
• Biological source: MUS MUSCULUS (HOUSE MOUSE)
• Cellular location: Isoform Mt-VDAC1: Mitochondrion outer membrane; Multi-pass membrane protein. Isoform Pl-VDAC1: Cell membrane; Multi-pass membrane protein: Q60932
• Total number of polymer chains: 1
• Total formula weight: 35435.40

Authors

Paz, A.,Colletier, J.P.,Abramson, J. (deposition date: 2013-09-17, release date: 2014-06-04, Last modification date: 2023-12-20)

Primary citation

Choudhary, O.P.,Paz, A.,Adelman, J.L.,Colletier, J.,Abramson, J.,Grabe, M.
Structure-Guided Simulations Illuminate the Mechanism of ATP Transport Through Vdac1.
Nat.Struct.Mol.Biol., 21:626-, 2014

PubMed Abstract: The voltage-dependent anion channel (VDAC) mediates the flow of metabolites and ions across the outer mitochondrial membrane of all eukaryotic cells. The open channel passes millions of ATP molecules per second, whereas the closed state exhibits no detectable ATP flux. High-resolution structures of VDAC1 revealed a 19-stranded β-barrel with an α-helix partially occupying the central pore. To understand ATP permeation through VDAC, we solved the crystal structure of mouse VDAC1 (mVDAC1) in the presence of ATP, revealing a low-affinity binding site. Guided by these coordinates, we initiated hundreds of molecular dynamics simulations to construct a Markov state model of ATP permeation. These simulations indicate that ATP flows through VDAC through multiple pathways, in agreement with our structural data and experimentally determined physiological rates.

PubMed: 24908397
DOI: 10.1038/NSMB.2841

Experimental method

X-RAY DIFFRACTION (2.277 Å)