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 with one interwoven beta sheet. 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 with one interwoven beta sheet. 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.

== Enzymatic Activity ==

Sandbox Reserved 1053: Difference between revisions

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@@ Line 8: / Line 8: @@
 == 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 with one interwoven beta sheet. 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 with one interwoven beta sheet. 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.
 == Enzymatic Activity ==