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The important residues for ATP hydrolysis and/or binding are located in the P-loop. The ATP-binding pocket is located at the extremity of armI. The perpendicular armII contains mostly the alpha helical subdomain with the signature motif. It only seems to be required for structural integrity of the ABC module. ArmII is in direct contact with the ...
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 ...
The ATP binding site is the environment in which ATP catalytically actives the enzyme and, as a result, is hydrolyzed to ADP. [2] The binding of ATP causes a conformational change to the enzyme it is interacting with. [3] The genetic and functional similarity of such a motif demonstrates micro-evolution: proteins have co-opted the same binding ...
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
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 ...
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]
The Walker A and Walker B motifs are protein sequence motifs, known to have highly conserved three-dimensional structures. These were first reported in ATP-binding proteins by Walker and co-workers in 1982. [1] Of the two motifs, the A motif is the main "P-loop" responsible for binding phosphate, while the B motif is a much less conserved ...
ATP-binding cassette super-family G member 2 is a protein that in humans is encoded by the ABCG2 gene. [ 6 ] [ 7 ] ABCG2 has also been designated as CDw338 ( cluster of differentiation w338). ABCG2 is a translocation protein used to actively pump drugs and other compounds against their concentration gradient using the bonding and hydrolysis of ...