Problem Set 5 Key

2 glycosyltransferases 25 points a charnock davies

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Unformatted text preview: different combinations that can occur, N- C or C- N for amino acids and 3’- 5’ or 5’- 3’ for nucleic acids. However, carbohydrates have multiple attachment sites throughout their chemical structure due to the numerous hydroxyl groups found within carbohydrates that are available for intermolecular acetal formation. This allows for many different glycosidic linkages that can potentially be formed between the anomeric carbon of one monosaccharide and any one of the hydroxyl groups in another. 2. Glycosyltransferases (25 points): a. Charnock & Davies (1999, Biochemistry, 38, 6380- 6385) suggested a possible catalytic mechanism of SpsA, a glycosyltransferase involved in the production of the mature spore coat in Bacillus subtilis, by comparing 2 crystal structures with different divalent metal ions. i. Describe what GT- A fold is using the SpsA crystal structure (PDB ID: 1QGQ). Make a figure if necessary to indicate some features of the GT- A fold. Why is this fold important? (3 points) The GT- A fold consists of two tightly associated β/α/β (Rossmann- like) folds as shown in overall structure of BsSpsA below. It contains two different domains for N- terminal nucleotide binding (resi 2- 100) and C- terminal substrate binding (resi 101- 256). Also, a DXD motif that coordinates a divalent cation (Mn2+) is a part of the GT- A fold. This fold is important in that it represents one of the two main folds discovered in families of glycosyltransferases, which are one of the largest and most diverse enzyme groups in living cells. ii. BsSpsA is the fir...
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