Sandbox Reserved 1070
From Proteopedia
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== Zinc Ligand(s) == | == Zinc Ligand(s) == | ||
| + | Most cells possess efficient Zinc uptake systems, as Zinc is a reactive Lewis Acid. Zinc binds incredibly tightly to this enzyme at subfemtomolar concentrations. The Zinc co-purified with the protein. | ||
=== Zinc Binding Site === | === Zinc Binding Site === | ||
| - | + | Zinc allosterically inhibits the activity of the enzyme, through an allosteric binding site located on the CZB domain of DgcZ. The CZB domain, where the Zinc binding sites are located, regulates the function of the GGDEF domain, containing the active site. CZB is the N-terminal domain, and is folded into four anti-parallel α-helices, as a 2-fold symmetric homodimer. Zinc coordinates to three amino acids spanning three of the four alpha helices in the CZB domain: the H22 residue of 𝝰1, C52 𝝰2, and H79 and H83 of 𝝰3,and 𝝰4 helix containing the N-terminus. When Zinc is removed from the CZB domain, using EDTA in methods, the 𝝰1 helix straightens burying nonpolar side-chain residues, which affect the activity of DgcZ. | |
| + | |||
== Other Ligands == | == Other Ligands == | ||
Revision as of 17:31, 17 March 2017
| This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080. |
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Contents |
DgcZ from E. coli
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This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Biological Function
Structural Overview
Mechanism of Action
Zinc Ligand(s)
Most cells possess efficient Zinc uptake systems, as Zinc is a reactive Lewis Acid. Zinc binds incredibly tightly to this enzyme at subfemtomolar concentrations. The Zinc co-purified with the protein.
Zinc Binding Site
Zinc allosterically inhibits the activity of the enzyme, through an allosteric binding site located on the CZB domain of DgcZ. The CZB domain, where the Zinc binding sites are located, regulates the function of the GGDEF domain, containing the active site. CZB is the N-terminal domain, and is folded into four anti-parallel α-helices, as a 2-fold symmetric homodimer. Zinc coordinates to three amino acids spanning three of the four alpha helices in the CZB domain: the H22 residue of 𝝰1, C52 𝝰2, and H79 and H83 of 𝝰3,and 𝝰4 helix containing the N-terminus. When Zinc is removed from the CZB domain, using EDTA in methods, the 𝝰1 helix straightens burying nonpolar side-chain residues, which affect the activity of DgcZ.
Other Ligands
Binding Site
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</StructureSection>
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
