Sandbox Reserved 1802

This Sandbox is Reserved from Mar 1 through Jun 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1796 through Sandbox Reserved 1811.

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Chorismate dehydratase (MqnA)

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function of your protein The specific function of my protein is catalyzing the dehydration of chorismate to yield 3-enolpyruvyl-benzoate (3-EPB), which is the initial step in the biosynthesis of menaquinone via the futalosine pathway. Biological relevance and broader implications Enzymes involved in this pathway are potential targets for the development of new antibiotics via this pathway, and enzymes that convert chorismate are promising targets for potential antimicrobials and herbicides. Important amino acids The three amnio acids involved in the catalytic triad. Important amino acids for binding are the following: I13, N17, C18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, Y242 Structural highlights Chorismate dehydratase’s secondary structures has roughly 19 beta sheets, 27 alpha helices, and several random coils. The tertiary structure would be described as globular as is it in a shape of a ball that includes an alpha clamp and two lobes connected by two linkers.