Marking Sugar’s Spot | Chemical & Engineering News
Volume 89 Issue 25 | p. 2 | Concentrates
Issue Date: June 20, 2011

Marking Sugar’s Spot

Department: Science & Technology
Keywords: carbohydrate, X-ray crystallography, post-translational modification
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Hydrogen bonding to anionic amino acids (green) from an enzyme (blue) readies a peptide substrate’s asparagine (red) for sugar transfer. The metal ion (pink) is manganese or magnesium.
Credit: Courtesy of Kaspar Locher
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Hydrogen bonding to anionic amino acids (green) from an enzyme (blue) readies a peptide substrate’s asparagine (red) for sugar transfer. The metal ion (pink) is manganese or magnesium.
Credit: Courtesy of Kaspar Locher

By using X-ray crystallography, researchers have learned how a sugar-transferring enzyme recognizes peptide sequences that trigger a common protein modification reaction—asparagine-linked glycosylation (Nature, DOI: 10.1038/nature10151). Saccharide attachment at asparagine’s side-chain nitrogen is important for protein folding, cell-cell communication, and more, but researchers know little about the attachment process. It requires either a serine or threonine to be two residues away from the asparagine to be modified, but it’s not clear how asparagine’s nitrogen, a poor nucleophile, gets activated for modification. To answer that question, Kaspar P. Locher, Christian Lizak, and coworkers at ETH Zurich crystallized a bacterial transferase together with a peptide substrate. They found that the hydroxyl-containing amino acid helps the enzyme recognize the substrate, but it doesn’t facilitate the reaction. That job belongs to an aspartate and a glutamate in the transferase, which juice up the asparagine by forming hydrogen bonds to its amide protons. The team says more structures need to be solved to fully understand the reaction.

 
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