Sandbox Reserved 1072: Difference between revisions

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== Structural Overview ==

[[Image:DgcZ full molecule all sites and ligands labeled.png|250 px|left|thumb|Diguanylate cyclase DgcZ from “E. Coli” with Domains Labeled]]

The DgcZ protein has C2 symmetry ~~composed of two domains~~. The catalytic glycine-glycine-glutamate-glutamate-phenylalanine (GGEEF) domain responsible for synthesizing c-di-GMP and the regulatory chemoreceptor zinc binding (CZB) domain comprising two zinc binding sites. DgcZ binds zinc with sub-femtomolar affinity. When zinc is bound, the CZB and GGEEF domains adopt conformations that inhibit DgcZ function [1]. Enzyme DgcZ was co-crystallized with Zinc fixing the structure in its inactivate conformation. The CZB domain is common to many bacterial lineages, including its prevalence in DgcZ homologs. The domain has an important role in signal transduction of bacteria. CZB and GGEEF domains are prevalent in many bacterial proteins from differing strands of ''E. coli'' [2]~~. DgcZ is a protein from ''E. coli'' made of two domains each of which is a symmetric homodimer. It exhibits <scene name='69/694239/C2_symmetry/6'>C2</scene> symmetry down its central axis~~. The GGEEF domain is catalytic in that it contains the active sites used for cyclizing GTP into c-di-GMP. The CZB domain is used for ligand-mediated regulation of c-di-GMP production.

DgcZ is a tetrameric protein from ''E. coli'' made of two domains. Each domain is a dimer, so the whole protein can be called a dimer of dimers. The DgcZ protein has <scene name='69/694239/C2_symmetry/6'>C2</scene> symmetry down its central axis. The catalytic glycine-glycine-glutamate-glutamate-phenylalanine (GGEEF) domain is responsible for synthesizing c-di-GMP, and the regulatory chemoreceptor zinc binding (CZB) domain comprising two zinc binding sites. DgcZ binds zinc with sub-femtomolar (10-16M) affinity. When zinc is bound, the CZB and GGEEF domains adopt conformations that inhibit DgcZ function [1]. Enzyme DgcZ was co-crystallized with Zinc fixing the structure in its inactivate conformation. The CZB domain is common to many bacterial lineages, including its prevalence in DgcZ homologs. The domain has an important role in signal transduction of bacteria. CZB and GGEEF domains are prevalent in many bacterial proteins from differing strands of ''E. coli'' [2]. The GGEEF domain is catalytic in that it contains the active sites used for cyclizing GTP into c-di-GMP. The CZB domain is used for ligand-mediated regulation of c-di-GMP production.

===Catalytic GGEEF Domain===

Sandbox Reserved 1072: Difference between revisions

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 == Structural Overview ==
 [[Image:DgcZ full molecule all sites and ligands labeled.png|250 px|left|thumb|Diguanylate cyclase DgcZ from “E. Coli” with Domains Labeled]]
-The DgcZ protein has C2 symmetry composed of two domains. The catalytic glycine-glycine-glutamate-glutamate-phenylalanine (GGEEF) domain responsible for synthesizing c-di-GMP and the regulatory chemoreceptor zinc binding (CZB) domain comprising two zinc binding sites. DgcZ binds zinc with sub-femtomolar affinity. When zinc is bound, the CZB and GGEEF domains adopt conformations that inhibit DgcZ function <sup>[1]</sup>. Enzyme DgcZ was co-crystallized with Zinc fixing the structure in its inactivate conformation. The CZB domain is common to many bacterial lineages, including its prevalence in DgcZ homologs. The domain has an important role in signal transduction of bacteria. CZB and GGEEF domains are prevalent in many bacterial proteins from differing strands of ''E. coli'' <sup>[2]</sup>. DgcZ is a protein from ''E. coli'' made of two domains each of which is a symmetric homodimer. It exhibits <scene name='69/694239/C2_symmetry/6'>C2</scene> symmetry down its central axis. The GGEEF domain is catalytic in that it contains the active sites used for cyclizing GTP into c-di-GMP. The CZB domain is used for ligand-mediated regulation of c-di-GMP production.
+DgcZ is a tetrameric protein from ''E. coli'' made of two domains. Each domain is a dimer, so the whole protein can be called a dimer of dimers. The DgcZ protein has <scene name='69/694239/C2_symmetry/6'>C2</scene> symmetry down its central axis. The catalytic glycine-glycine-glutamate-glutamate-phenylalanine (GGEEF) domain is responsible for synthesizing c-di-GMP, and the regulatory chemoreceptor zinc binding (CZB) domain comprising two zinc binding sites. DgcZ binds zinc with sub-femtomolar (10<sup>-16</sup>M) affinity. When zinc is bound, the CZB and GGEEF domains adopt conformations that inhibit DgcZ function <sup>[1]</sup>. Enzyme DgcZ was co-crystallized with Zinc fixing the structure in its inactivate conformation. The CZB domain is common to many bacterial lineages, including its prevalence in DgcZ homologs. The domain has an important role in signal transduction of bacteria. CZB and GGEEF domains are prevalent in many bacterial proteins from differing strands of ''E. coli'' <sup>[2]</sup>. The GGEEF domain is catalytic in that it contains the active sites used for cyclizing GTP into c-di-GMP. The CZB domain is used for ligand-mediated regulation of c-di-GMP production.
 ===Catalytic GGEEF Domain===