Sandbox Reserved 1053: Difference between revisions

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== General Structure ==

Antigen 85C was crystallized in its dimeric form.<ref>PMID: 25028518</ref> The <scene name='69/694220/Secondary_structures/2'>secondary structure</scene> shown in the monomeric form is composed of helices, shown in pink, with one interwoven beta sheet, shown in yellow. ~~Due to the serine hydrolase activity~~ of ~~Ag85C, the enzyme contains a α/β hydrolase fold with~~ a central β-sheet bordered by α–helices, and this tertiary conformation is highly conserved across enzymes that function in this capacity. <ref>PMID:10655617</ref> The substrate binding pocket of Ag85C is composed of two separate but equally important components; there is carbohydrate binding pocket for the trehalose, and there is a fatty acid binding pocket for the mycolic acid. As a result, trahalose monomycolate can effectively bind to the Ag85C binding pocket.

Antigen 85C was crystallized in its dimeric form.<ref>PMID: 25028518</ref> The <scene name='69/694220/Secondary_structures/2'>secondary structure</scene> shown in the monomeric form is composed of helices, shown in pink, with one interwoven beta sheet, shown in yellow. The confrontation of a central β-sheet bordered by α–helices creates an a α/β hydrolase fold in Ag85C, and this tertiary conformation is highly conserved across enzymes that function in this capacity. <ref>PMID:10655617</ref> The substrate binding pocket of Ag85C is composed of two separate but equally important components; there is carbohydrate binding pocket for the trehalose, and there is a fatty acid binding pocket for the mycolic acid. As a result, trahalose monomycolate can effectively bind to the Ag85C binding pocket.

== Enzymatic Activity ==

Sandbox Reserved 1053: Difference between revisions

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 == General Structure ==
-Antigen 85C was crystallized in its dimeric form.<ref>PMID: 25028518</ref> The <scene name='69/694220/Secondary_structures/2'>secondary structure</scene> shown in the monomeric form is composed of helices, shown in pink, with one interwoven beta sheet, shown in yellow. Due to the serine hydrolase activity of Ag85C, the enzyme contains a α/β hydrolase fold with a central β-sheet bordered by α–helices, and this tertiary conformation is highly conserved across enzymes that function in this capacity. <ref>PMID:10655617</ref> The substrate binding pocket of Ag85C is composed of two separate but equally important components; there is carbohydrate binding pocket for the trehalose, and there is a fatty acid binding pocket for the mycolic acid. As a result, trahalose monomycolate can effectively bind to the Ag85C binding pocket.
+Antigen 85C was crystallized in its dimeric form.<ref>PMID: 25028518</ref> The <scene name='69/694220/Secondary_structures/2'>secondary structure</scene> shown in the monomeric form is composed of helices, shown in pink, with one interwoven beta sheet, shown in yellow. The confrontation of a central β-sheet bordered by α–helices creates an a α/β hydrolase fold in Ag85C, and this tertiary conformation is highly conserved across enzymes that function in this capacity. <ref>PMID:10655617</ref> The substrate binding pocket of Ag85C is composed of two separate but equally important components; there is carbohydrate binding pocket for the trehalose, and there is a fatty acid binding pocket for the mycolic acid. As a result, trahalose monomycolate can effectively bind to the Ag85C binding pocket.
 == Enzymatic Activity ==