ATP-binding motif

An ATP, adenosine triphosphate, binding motif is a 250 residue sequence within an ATP binding protein’s primary structure. The binding motif is associated with a protein’s structure and/or function. ATP is a molecule of energy, and can be a coenzyme, involved in a number of biological reactions. ATP is proficient at interacting with other molecules through a binding site. The ATP binding site is the environment in which ATP catalytically actives the enzyme and, as a result, is hydrolyzed to ADP. The binding of ATP causes a conformational change to the enzyme it is interacting with. An ATP, adenosine triphosphate, binding motif is a 250 residue sequence within an ATP binding protein’s primary structure. The binding motif is associated with a protein’s structure and/or function. ATP is a molecule of energy, and can be a coenzyme, involved in a number of biological reactions. ATP is proficient at interacting with other molecules through a binding site. The ATP binding site is the environment in which ATP catalytically actives the enzyme and, as a result, is hydrolyzed to ADP. The binding of ATP causes a conformational change to the enzyme it is interacting with. The genetic and functional similarity of such a motif demonstrates micro-evolution: proteins have co-opted the same binding sequence from other enzymes rather than developing them independently. ATP binding sites, which may be representative of an ATP binding motif, are present in many proteins which require an input of energy (from ATP), such sites as active membrane transporters, microtubule subunits, flagellum proteins, and various hydrolytic and proteolytic enzymes. The short motifs involving ATP-binding are the Walker A, also known as the P-loop, Walker B, Signature, and switch motif. The Walker site A has a primary amino acid sequence of GXXGXFKS(or T). The letter X can represent any amino acid. The primary amino acid sequence of the Walker B site is hhhhD, in which h represents any hydrophobic amino acid. The C motif, also known as the Signature motif, LSGGQ motif, or the linker peptide, has a primary amino acid sequence of LSGGQQ/R/KQR. Due to the variety of different amino acids that can be used in the primary sequence, of both the Walker site A and B, the non-variant amino acids within the sequence are highly conserved. A mutation of any of these amino acids will affect the binding ATP or interfere with the catalytic activity of the enzyme. The primary amino acid sequence determines the three dimensional structure of each motif. All of the ATP binding domains are made up of an estimated 250 residues and two subunits, creating a dimer. These residues are folded into six α-helices and five β-strands.