Sandbox Reserved 1072: Difference between revisions
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The <scene name='69/694239/Zb_domain_residues_19-90/4'>CZB Domain</scene>, residues 19-90, is responsible for regulating the function of DgcZ. The domain contains the allosteric binding site of the enzyme with cooperative binding. Four residues bind zinc with a high affinity even at 10<sup>-16M</sup> concentrations. Due to the tightness of Zinc binding, the enzyme has not yet been crystallized in the active conformation without the presence of Zinc metal inhibitor. When zinc is bound, DgcZ activity is limited<sup>[1]</sup>. | The <scene name='69/694239/Zb_domain_residues_19-90/4'>CZB Domain</scene>, residues 19-90, is responsible for regulating the function of DgcZ. The domain contains the allosteric binding site of the enzyme with cooperative binding. Four residues bind zinc with a high affinity even at 10<sup>-16M</sup> concentrations. Due to the tightness of Zinc binding, the enzyme has not yet been crystallized in the active conformation without the presence of Zinc metal inhibitor. When zinc is bound, DgcZ activity is limited<sup>[1]</sup>. | ||
[[Image: | [[Image:zinc binding site.jpg|250 px|left|thumb|Zn<sup>+2</sup> Coordination to amino acid residues on three of the four 𝝰 helices of DgcZ]] | ||
[[Image:Electrostatic map front view CZB.png|250 px|right|thumb|Electrostatic potential map of the CZB domain of Diguanylate Cyclase. Regions of relatively negative charge are in red and regions of relatively positive charge are in blue. Electrically neutral regions are in white]] | [[Image:Electrostatic map front view CZB.png|250 px|right|thumb|Electrostatic potential map of the CZB domain of Diguanylate Cyclase. Regions of relatively negative charge are in red and regions of relatively positive charge are in blue. Electrically neutral regions are in white]] | ||
=== Zinc Binding Site === | === Zinc Binding Site === | ||
