Sandbox Reserved 796

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This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807.

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spinqualitylabelsall models Fructose-1,6-bisphosphate aldolase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Contents 1 Introduction and General Structure 2 Hydrogen and Disulfide Bond 3 Hydrophobic and Hydrophilic Residues 4 Solvent 5 The ligands and ligand contacts 6 Catalytic Residues 7 References

Introduction and General Structure

is an enzyme in glycolysis, the metabolic pathway that converts glucose into pyruvate and produces cellular energy in form of ATP (adenosine triphosphate). Aldolase catalyzes an aldol cleavage reaction that hydrolyzes fructose 1,6-bisphosphate. Fructose-1,6-bisphosphate aldolase is a tetramer, has alpha helices in pinkish purple and beta sheets in blue. The alpha helices are mostly found on the surface (outside) of the enzyme while the beta sheets are embedded in the inside of the enzyme.

Hydrogen and Disulfide Bond

are in black and there is no observable disulfide bond in the enzyme. Based on the position of the Hydrogen bonds, we concluded that the beta sheets are parallel to each other since the H-bonds are slanted.

Hydrophobic and Hydrophilic Residues

The are in orange while the are in teal. Based on this model, we can conclude that the enzyme is made out of a roughly equal amount of both hydrophobic and hydrophilic residues.

Solvent

(colored in cream) surrounded the enzyme, which indicated that the residues that made up the surface of the enzyme is hydrophilic. With 50% transparency, no water molecules is observed to be inside the enzyme, which indicated that the inner surface of the enzyme must be hydrophobic.

The ligands and ligand contacts

is in purple. There are three other ligands in the other subunits (B, C, and D).

Catalytic Residues

are Asn33(A)-Glu187(A)-Lys229(A)(in red)

References