Sentence examples for binding of the phosphate from inspiring English sources

Interestingly, the human structure most closely resembles the inhibitor-bound structure, suggesting that binding of the phosphate moiety of the substrate may trigger this conformational change.

In addition, a well-defined water molecule (wat1) mediates binding of the phosphate group of PLP to the side chains of K241 and H215 from the opposite subunit.

Another water molecule (wat2) also mediates binding of the phosphate group of PLP to the side chain of E194 and the main chain amide and carbonyl oxygen of G195 as observed previously in the cofactor bound structures of ArnB.

The substrate binding site of the bovine mitochondrial ADP/ATP carrier has been proposed to consist of G182, I183 and Y186 for binding of the adenine moiety and R79, K22 and R279 for binding of the phosphate groups [14], [15], [16], [17], [18], which could form an aromatic stacking and three ionic interactions with ADP, consistent with this idea.

For example, the Walker GXXXXGKT/S motif (X denotes any residue) can coordinate binding of the phosphate of ATP (Walker et al., 1982), and a Q-motif comprising a conserved glutamine and an aromatic amino acid 17 amino acids upstream can contribute to adenine binding (Tanner et al., 2003).

In the model, it seems most likely that the conserved lysine residues contribute to binding of the phosphate of ATP as cysteine mutants of these residues show that ATP potency can be increased by positively charged MTS reagents and reduced by negatively charged MTS reagents (Roberts and Evans, 2007; Roberts et al., 2008).

The binding of this phosphate helps in orienting the pT moiety of the substrate into the catalytic pocket of the enzyme (Li et al. 2007).

The corresponding lysine residues in several Fatty Acyl-CoA Synthetases have been implicated in the binding to the phosphate group of ATP via electrostatic interactions [21].

Apart from helix 3, we observe sequence-specific interactions from residues in the α1 α2 loop (Y291 binding to the phosphate O of G7) and the N-terminal arm.

RNase' A active sites can be divided in different subsites corresponding to the binding sites of the phosphate (P0-Pn), base (B0-Bn) and ribose (R0-Rn) moieties of each RNA nucleotide (reviewed in [ 40]).

It is not clear whether binding of these phosphate ions, presumably from the crystallisation buffer, is biologically relevant.