| Value |
42
%
|
| Organism |
Mitochondria |
| Reference |
Choudhary OP, Paz A, Adelman JL, Colletier JP, Abramson J, Grabe M. Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1. Nat Struct Mol Biol. 2014 Jul21(7):626-32. doi: 10.1038/nsmb.2841 p.628 left column 2nd paragraphPubMed ID24908397
|
| Primary Source |
[23] Rostovtseva TK, Bezrukov SM. ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis. Biophys J. 1998 May74(5):2365-73 DOI: 10.1016/S0006-3495(98)77945-7PubMed ID9591663
|
| Method |
Abstract: "To understand ATP permeation through VDAC, [investigators] solved the crystal structure of mouse VDAC1 (mVDAC1) in the presence of ATP, revealing a low-affinity binding site. Guided by these coordinates, [they] initiated hundreds of molecular dynamics simulations to construct a Markov state model of ATP permeation." |
| Comments |
P.628 left column 2nd paragraph: "The single-channel conductance values with and without ATP (determined from the slopes of the lines in Fig. 2b,c) are 3.04 and 5.24 nS, respectively. Thus, ATP reduced the conductance by 42%, results in excellent agreement with the experimental drop of 43% observed in single-channel currents under saturating ATP [primary source]." |
| Entered by |
Uri M |
| ID |
116637 |