Sandbox Reserved 1072: Difference between revisions

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[[Image:Poly B-1, 6 GlcNAc.jpg |175 px|left|thumb|'''Figure 2: Poly-β-1,6-N-acetylglucosamine.''' Poly-β-1,6-N-acetylglucosamine is a carbohydrate formed downstream of c-di-GMP utilized in formation of bacterial bio-films.]]

[[Image:DgcZ all domains sites labeled.png|250 px|left|thumb|'''Figure 4: Diguanylate cyclase DgcZ from ''E. Coli''.''' The domains of the enzyme are labeled, as well as the allosteric binding sites and the Zn+2 binding sites on the CZB domains[3].]]

DgcZ is a dimeric protein with ~~<scene name='69/694239/Dgcz_ggeef_dom_and_czb_dom/3'>~~two domains~~</scene>~~ per monomer[4]. 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) domains are responsible for synthesizing c-di-GMP. The regulatory chemoreceptor Zinc binding (CZB) domains house the two zinc binding sites, one site located on each monomer. DgcZ binds Zinc in the CZB domains with sub-femtomolar (10-16M) affinity. When Zinc is bound, the CZB and GGEEF domains adopt conformations that inhibit DgcZ function, as illustrated in Figure 3[3]. Enzyme DgcZ was co-crystallized with Zinc, fixing the structure in its inactivate conformation. The GGEEF domains are catalytic, containing the active sites for cyclizing GTP into c-di-GMP. The CZB domains are used for ligand-mediated regulation of c-di-GMP production and have an important role in signal transduction of bacteria. CZB and GGEEF domains are found in proteins from many bacterial lineages, including DgcZ homologs[5].

DgcZ is a dimeric protein with two domains per monomer[4]. 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) domains are responsible for synthesizing c-di-GMP. The regulatory chemoreceptor Zinc binding (CZB) domains house the two zinc binding sites, one site located on each monomer. DgcZ binds Zinc in the CZB domains with sub-femtomolar (10-16M) affinity. When Zinc is bound, the CZB and GGEEF domains adopt conformations that inhibit DgcZ function, as illustrated in Figure 3[3]. Enzyme DgcZ was co-crystallized with Zinc, fixing the structure in its inactivate conformation. The GGEEF domains are catalytic, containing the active sites for cyclizing GTP into c-di-GMP. The CZB domains are used for ligand-mediated regulation of c-di-GMP production and have an important role in signal transduction of bacteria. <scene name='69/694239/Dgcz_ggeef_dom_and_czb_dom/3'>CZB and GGEEF domains</scene> are found in proteins from many bacterial lineages, including DgcZ homologs[5].

==Catalytic GGEEF Domains==

Sandbox Reserved 1072: Difference between revisions

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 [[Image:Poly B-1, 6 GlcNAc.jpg |175 px|left|thumb|'''Figure 2: Poly-β-1,6-N-acetylglucosamine.''' Poly-β-1,6-N-acetylglucosamine is a carbohydrate formed downstream of c-di-GMP utilized in formation of bacterial bio-films.]]
 [[Image:DgcZ all domains sites labeled.png|250 px|left|thumb|'''Figure 4: Diguanylate cyclase DgcZ from ''E. Coli''.''' The domains of the enzyme are labeled, as well as the allosteric binding sites and the Zn<sup>+2</sup> binding sites on the CZB domains<sup>[3]</sup>.]]
-DgcZ is a dimeric protein with <scene name='69/694239/Dgcz_ggeef_dom_and_czb_dom/3'>two domains</scene> per monomer<sup>[4]</sup>. 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) domains are responsible for synthesizing c-di-GMP. The regulatory chemoreceptor Zinc binding (CZB) domains house the two zinc binding sites, one site located on each monomer. DgcZ binds Zinc in the CZB domains with sub-femtomolar (10<sup>-16</sup>M) affinity. When Zinc is bound, the CZB and GGEEF domains adopt conformations that inhibit DgcZ function, as illustrated in Figure 3<sup>[3]</sup>. Enzyme DgcZ was co-crystallized with Zinc, fixing the structure in its inactivate conformation. The GGEEF domains are catalytic, containing the active sites for cyclizing GTP into c-di-GMP. The CZB domains are used for ligand-mediated regulation of c-di-GMP production and have an important role in signal transduction of bacteria. CZB and GGEEF domains are found in proteins from many bacterial lineages, including DgcZ homologs<sup>[5]</sup>.
+DgcZ is a dimeric protein with two domains per monomer<sup>[4]</sup>. 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) domains are responsible for synthesizing c-di-GMP. The regulatory chemoreceptor Zinc binding (CZB) domains house the two zinc binding sites, one site located on each monomer. DgcZ binds Zinc in the CZB domains with sub-femtomolar (10<sup>-16</sup>M) affinity. When Zinc is bound, the CZB and GGEEF domains adopt conformations that inhibit DgcZ function, as illustrated in Figure 3<sup>[3]</sup>. Enzyme DgcZ was co-crystallized with Zinc, fixing the structure in its inactivate conformation. The GGEEF domains are catalytic, containing the active sites for cyclizing GTP into c-di-GMP. The CZB domains are used for ligand-mediated regulation of c-di-GMP production and have an important role in signal transduction of bacteria. <scene name='69/694239/Dgcz_ggeef_dom_and_czb_dom/3'>CZB and GGEEF domains</scene> are found in proteins from many bacterial lineages, including DgcZ homologs<sup>[5]</sup>.
 ==Catalytic GGEEF Domains==