| Value |
5e+8
water molecules/sec
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Stroud RM, Miercke LJ, O'Connell J, Khademi S, Lee JK, Remis J, Harries W, Robles Y, Akhavan D. Glycerol facilitator GlpF and the associated aquaporin family of channels. Curr Opin Struct Biol. 2003 Aug13(4):424-31.PubMed ID12948772
|
| Primary Source |
M.J. Borgnia, D. Kozono, G. Calamita, P.C. Maloney and P. Agre, Functional reconstitution and characterization of AqpZ, the E. coli water channel protein. J Mol Biol 291 (1999), pp. 1169–1179.PubMed ID10518952
|
| Method |
The mechanism of water conduction through AQP channels is suggested by the crystal structure of GlpF with water alone in the channel. Visualized at 2.7 Å resolution, the observed water positions can be compared with those in a molecular simulation. Seven to nine water molecules form a single file in the 20 Å constriction region of the channel. |
| Comments |
The calculated diffusion constant corresponds to a flux of 2.4 × 10^9 s-1, , which is just five times larger than the experimental flux for GlpF of 0.5 × 10^9 s-1. Here given is the experimental value |
| Entered by |
Uri M |
| ID |
103684 |