Sandbox Reserved 1070: Difference between revisions

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===Catalytic GGEEF Domain===

The GGEEF domain ~~includes a central five-stranded β-sheet surrounded by five α-helices. The~~ GGDEF ~~domain~~ includes a conserved sequence of GG[DE][DE]F [2]. Each dimer contains an active half-site that, when combined together in a productive conformation, form the entire active site. Each half-site binds one GTP molecule. The guanyl base forms hydrogen bonds with Asp-173 and Asn-182 to hold it in the active site. A Mg<sup>2+</sup> ion stabilizes the negative charges on the phosphate groups. When in the productive conformation, each GTP is held in close proximity with the α-phosphate groups overlapping C3 of the ribose. This conformation allows the α-phospate of one GTP to react with the alcohol group on C3 of the ribose of the other GTP, resulting in a cyclization of the two molecules into c-di-GMP. The ribose of each guanosine triphosphate, and subsequent product c-di-GMP riboses, are held only loosely by the enzyme, while the phosphate groups are not bound at all.

The GGEEF domain of DgcZ is part of the GGDEF family of proteins that includes a conserved sequence, GG[DE][DE]F[2].The GGEEF domain is a homodimer consisting of a central five-stranded β-sheet surrounded by five α-helices. Each dimer contains an active half-site that, when combined together in a productive conformation, form the entire active site. Each half-site binds one GTP molecule. The guanyl base forms hydrogen bonds with Asp-173 and Asn-182 to hold it in the active site. A Mg<sup>2+</sup> ion stabilizes the negative charges on the phosphate groups. When in the productive conformation, each GTP is held in close proximity with the α-phosphate groups overlapping C3 of the ribose. This conformation allows the α-phospate of one GTP to react with the alcohol group on C3 of the ribose of the other GTP, resulting in a cyclization of the two molecules into c-di-GMP. The ribose of each guanosine triphosphate, and subsequent product c-di-GMP riboses, are held only loosely by the enzyme, while the phosphate groups are not bound at all.

===Mechanism of Action===

Sandbox Reserved 1070: Difference between revisions

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 ===Catalytic GGEEF Domain===
-The GGEEF domain includes a central five-stranded β-sheet surrounded by five α-helices. The GGDEF domain includes a conserved sequence of GG[DE][DE]F [2]. Each dimer contains an active half-site that, when combined together in a productive conformation, form the entire active site. Each half-site binds one GTP molecule. The guanyl base forms hydrogen bonds with Asp-173 and Asn-182 to hold it in the active site. A Mg<sup>2+</sup> ion stabilizes the negative charges on the phosphate groups. When in the productive conformation, each GTP is held in close proximity with the α-phosphate groups overlapping C3 of the ribose. This conformation allows the α-phospate of one GTP to react with the alcohol group on C3 of the ribose of the other GTP, resulting in a cyclization of the two molecules into c-di-GMP. The ribose of each guanosine triphosphate, and subsequent product c-di-GMP riboses, are held only loosely by the enzyme, while the phosphate groups are not bound at all.
+The GGEEF domain of DgcZ is part of the GGDEF family of proteins that includes a conserved sequence, GG[DE][DE]F[2].The GGEEF domain is a homodimer consisting of a central five-stranded β-sheet surrounded by five α-helices. Each dimer contains an active half-site that, when combined together in a productive conformation, form the entire active site. Each half-site binds one GTP molecule. The guanyl base forms hydrogen bonds with Asp-173 and Asn-182 to hold it in the active site. A Mg<sup>2+</sup> ion stabilizes the negative charges on the phosphate groups. When in the productive conformation, each GTP is held in close proximity with the α-phosphate groups overlapping C3 of the ribose. This conformation allows the α-phospate of one GTP to react with the alcohol group on C3 of the ribose of the other GTP, resulting in a cyclization of the two molecules into c-di-GMP. The ribose of each guanosine triphosphate, and subsequent product c-di-GMP riboses, are held only loosely by the enzyme, while the phosphate groups are not bound at all.
 ===Mechanism of Action===