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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 1 DgcZ from E. coli 2 Structural Overview 2.1 GGDEF Domain 2.2 CZB Domain 3 Mechanism of Action 4 Zinc Ligand(s) 5 Other Ligands 6 References

DgcZ from E. coli

Diguanylate cyclases synthesize cyclic dimeric-GMP (c-di-GMP) from two GTP molecules. C-di-GMP is a second messenger in the production of poly-β-1,6-N-acetylglucosamine (poly-GlcNAc) , a polysaccharide required for E. coli biofilm production. This biofilm allows E. coli to adhere to extracellular surfaces. The DgcZ protein is made of two domains: the catalytic GGDEF domain responsible for sythnesizing c-di-GMP and the regulatory CZB domain that binds zinc. When zinc is bound, the CZB and GGDEF domains adopt conformations that inhibit DgcZ function.

spinqualitylabelsall models E. coli Diguanylate cyclase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structural Overview

GGDEF Domain

CZB Domain

Mechanism of Action

Zinc Ligand(s)

Other Ligands

References