User:Youngsen Jeng: Difference between revisions

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Structural stabilization of Glutamine Synthetase by divalent cations, especially by the n1 ion<'''Insert wiki here'''>, has been ascribed to the attraction of their positive charges to the negative charges of glutamate and ATP and of their ligands<'''Insert wiki here'''> (Liaw et al., 1993~).

The structure of the dodecamer exposes several alpha loops which are important in stabilizing quaternary structure of Glutamine Synthetase. One beta loop consists of hydrophilic residues 156-173,<insert wiki> projects into the central channel of the dodecamer. Another beta loop is the adenylylation loop<insert wiki>, so called because it contains tyrosyine residue 397 which is covalently modified by addition of AMP. The amino group of glutamate shifts the Asn-264 loop, helping Ser-53P, on the Asp-50P loop, to stabilize the flap<insert wiki>.

The structure of the dodecamer exposes several alpha loops which are important in stabilizing quaternary structure of Glutamine Synthetase. One beta loop consists of hydrophilic residues 156-173,<insert wiki> projects into the central channel of the dodecamer. Another beta loop is the adenylylation loop<insert wiki>, so called because it contains tyrosyine residue 397 which is covalently modified by addition of AMP. The amino group of glutamate shifts the Asn-264 loop, helping Ser-53P, on the Asp-50P loop, to stabilize the flap<insert wiki>.downward extension of the two-stranded beta sheet whose strands are connected by the "Trp 57 loop."<insert wiki> These two strands complete the cylindrical active site of the neighboring subunit.(This neighbor is the one clockwise to the subunit, when the molecule is viewed down the 6-fold axis. That is, the Trp-57 loop of subunit F of completes the active site of subunit A)

=References=

User:Youngsen Jeng: Difference between revisions

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 Structural stabilization of Glutamine Synthetase by divalent cations, especially by the n1 ion<'''Insert wiki here'''>, has been ascribed to the attraction of their positive charges to the negative charges of glutamate and ATP and of their ligands<'''Insert wiki here'''> (Liaw et al., 1993~).
-The structure of the dodecamer exposes several alpha loops which are important in stabilizing quaternary structure of Glutamine Synthetase. One beta loop consists of hydrophilic residues 156-173,<insert wiki> projects into the central channel of the dodecamer. Another beta loop is the adenylylation loop<insert wiki>, so called because it contains tyrosyine residue 397 which is covalently modified by addition of AMP. The amino group of glutamate shifts the Asn-264 loop, helping Ser-53P, on the Asp-50P loop, to stabilize the flap<insert wiki>.
+The structure of the dodecamer exposes several alpha loops which are important in stabilizing quaternary structure of Glutamine Synthetase. One beta loop consists of hydrophilic residues 156-173,<insert wiki> projects into the central channel of the dodecamer. Another beta loop is the adenylylation loop<insert wiki>, so called because it contains tyrosyine residue 397 which is covalently modified by addition of AMP. The amino group of glutamate shifts the Asn-264 loop, helping Ser-53P, on the Asp-50P loop, to stabilize the flap<insert wiki>.downward extension of the two-stranded beta sheet whose strands are connected by the "Trp 57 loop."<insert wiki> These two strands complete the cylindrical active site of the neighboring subunit.(This neighbor is the one clockwise to the subunit, when the molecule is viewed down the 6-fold axis. That is, the Trp-57 loop of subunit F of completes the active site of subunit A)
 =References=
 <references/>