Sandbox Reserved 1072: Difference between revisions
From Proteopedia
Jump to navigationJump to search
David Emch (talk | contribs) No edit summary |
David Emch (talk | contribs) No edit summary |
||
| Line 10: | Line 10: | ||
== Structural Overview == | == Structural Overview == | ||
[[Image:DgcZ | [[Image:DgcZ all domains sites labeled.png|250 px|left|thumb|'''Figure 4: Diguanylate cyclase DgcZ from ''E. Coli''.''' The two domains of the enzyme are labeled]] | ||
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. 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 used 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 <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. 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 used 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>. | ||
