Search results
Results From The WOW.Com Content Network
A model that describes the conformational changes in the nucleotide-binding domain (NBD) as a result of ATP binding and hydrolysis is the ATP-switch model. This model presents two principal conformations of the NBDs: formation of a closed dimer upon binding two ATP molecules and dissociation to an open dimer facilitated by ATP hydrolysis and ...
In molecular biology, the ATP-grasp fold is a unique ATP-binding protein structural motif made of two α+β subdomains that "grasp" a molecule of ATP between them. ATP-grasp proteins have ATP-dependent carboxylate-amine/thiol ligase activity.
These proteins have receptors that bind to specific molecules (e.g., glucose) and transport them across the cell membrane. Because energy is required in this process, it is known as 'active' transport. Examples of active transport include the transportation of sodium out of the cell and potassium into the cell
A prokaryotic ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli is a heterotrimeric complex that interacts with an extracytoplasmic substrate binding protein to mediate the uptake of ...
The binding of a divalent cation, almost always magnesium, strongly affects the interaction of ATP with various proteins. Due to the strength of the ATP-Mg 2+ interaction, ATP exists in the cell mostly as a complex with Mg 2+ bonded to the phosphate oxygen centers. [6] [8] A second magnesium ion is critical for ATP binding in the kinase domain. [9]
P-gp is a 170 kDa transmembrane glycoprotein, which includes 10–15 kDa of N-terminal glycosylation.The N-terminal half of the protein contains six transmembrane helixes, followed by a large cytoplasmic domain with an ATP-binding site, and then a second section with six transmembrane helixes and an ATP-binding domain that shows over 65% of amino acid similarity with the first half of the ...
Myosin II is an elongated protein that is formed from two heavy chains with motor heads and two light chains. Each myosin head contains actin and ATP binding site. The myosin heads bind and hydrolyze ATP, which provides the energy to walk toward the plus end of an actin filament. Myosin II are also vital in the process of cell division. For ...
The P-type ATPases, also known as E 1-E 2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. [1] P-type ATPases are α-helical bundle primary transporters named based upon their ability to catalyze auto- (or self-) phosphorylation (hence P) of a key conserved aspartate residue within the pump and their energy source ...