Sandbox Reserved 1072: Difference between revisions

Line 11:

== 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]]

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 houses two zinc binding sites. DgcZ binds zinc in the CZB domain 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.

DgcZ is a tetrameric protein from ''E. coli'' made of <scene name='69/694239/Dgcz_ggeef_dom_and_czb_dom/1'>two domains</scene>. 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 houses two zinc binding sites. DgcZ binds zinc in the CZB domain 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

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 11: / Line 11: @@
 == 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]]
-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 houses two zinc binding sites. DgcZ binds zinc in the CZB domain 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.
+DgcZ is a tetrameric protein from ''E. coli'' made of <scene name='69/694239/Dgcz_ggeef_dom_and_czb_dom/1'>two domains</scene>. 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 houses two zinc binding sites. DgcZ binds zinc in the CZB domain 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===