EC Number |
Reaction |
Reference |
---|
5.6.1.6 | ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel |
- |
- |
5.6.1.6 | ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel |
asymmetric motion of the nucleotide binding domains 1 and 2 during channel gating. Opening of the channel is initiated by ATP at the nucleotide-binding domain 2 site, whereas separation of the nucleotide-binding domain dimer at the nucleotide-binding domain 1 site constitutes the rate-limiting step in channel closing |
688124 |
5.6.1.6 | ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel |
ATP binding, conformational changes, and ATPase and channel activity reaction mechanism, overview |
700618 |
5.6.1.6 | ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel |
regulation of CFTR activation by R domain phosphorylation followed by ATP binding at the nucleotide-binding domain-1 site enables the cycling mechanism to proceed. ATP catalysis at the catalytically active nucleotide?binding domain-2 is sufficient to drive the gating cycle, CFTR gating mechanism proceeds in 4 steps, detailed overview. The enzyme being a functional channel adapts the ATP switch gating mechanism designed for transporters, ATP Switch model analysis |
733100 |
5.6.1.6 | ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel |
the conformation of nucleotide-binding domain 1 changes before that of nucleotide-binding domain 2 during channel opening. Nucleotide-binding domain dimerization does not proceed by a symmetric tweezer-like motion, but instead in an asymmetric fashion led by nucleotide-binding domain1 |
689759 |
5.6.1.6 | ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel |
the conformation of nucleotide-binding domain1 changes before that of nucleotide-binding domain 2 during channel opening. Nucleotide-binding domain dimerization does not proceed by a symmetric tweezer-like motion, but instead in an asymmetric fashion led by nucleotide-binding domain1 |
689759 |
5.6.1.6 | ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel |
the structure of the CFTR channel pore is highly asymmetric with a narrower extracellular entrance and a dilating conformational change of the extracellular entrance is associated with the channel transition to a nonhydrolytic, locked-open state |
720313 |
5.6.1.6 | ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel |
upon channel opening, the wide cytoplasmic vestibule tightens and the pore-lining TM12 rotates along its helical axis |
720151 |