Transaldolase

PDB file 1UCW

This file depicts Transaldolase from E. Coli. The dihydroxyacetone moiety transferred by this enzyme forms a Schiff-base intermediate with the e-amino group of a lysine residue at the active site.  This intermediate has been reduced by borohydride prior to crystallization. The structure was solved by J. Jia, Y. Lindqvist, & G. Schneider, 1997.

Suggested display options:

To distinguish the 2 copies of the protein, color chain.
Display as
cartoon.
Now change the display to color
structure. Note the secondary structure.
Questions: What Glycolysis enzyme studied last semester has a similar structure?
What structural motif do these enzymes have in common?

,
Select hetero-ligand, display as ball & stick or sticks, and color CPK.
Try to distinguish atoms in the "ligand," formed by reduction of the Schiff base complex of  lysine132 with dihydroxyacetone.

Question: Is the active site at the same end of the barrel in this enzyme and the one you studied in the Glycolysis pathway?

Now display the protein as spacefill with color chain.
Questions: What part of the lysine-intermediate is exposed on the protein surface? Is this enzyme likely to function as a monomer?


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