6ZJ4

apo-Trehalose transferase (apo-TreT) from Thermoproteus uzoniensis

This is a non-PDB format compatible entry.

Summary for 6ZJ4

• Entry DOI: 10.2210/pdb6zj4/pdb
• Descriptor: Trehalose phosphorylase/synthase, THIOCYANATE ION (3 entities in total)
• Functional Keywords: trehalose transferase, retaining glycosyltransferase, glycosidic bond formation, transferase
• Biological source: Thermoproteus uzoniensis
• Total number of polymer chains: 1
• Total formula weight: 45619.48

Authors

Bento, I.,Mestrom, L.,Marsden, S.R.,van der Eijk, H.,Laustsen, J.U.,Jeffries, C.M.,Svergun, D.I.,Hagedoorn, P.-H.,Hanefeld, U. (deposition date: 2020-06-27, release date: 2020-09-30, Last modification date: 2024-01-31)

Primary citation

Mestrom, L.,Marsden, S.R.,van der Eijk, H.,Laustsen, J.U.,Jeffries, C.M.,Svergun, D.I.,Hagedoorn, P.L.,Bento, I.,Hanefeld, U.
Anomeric Selectivity of Trehalose Transferase with Rare l-Sugars.
Acs Catalysis, 10:8835-8839, 2020

PubMed Abstract: Retaining LeLoir glycosyltransferases catalyze the formation of glycosidic bonds between nucleotide sugar donors and carbohydrate acceptors. The anomeric selectivity of trehalose transferase from was investigated for both d- and l-glycopyranose acceptors. The enzyme couples a wide range of carbohydrates, yielding trehalose analogues with conversion and enantioselectivity of >98%. The anomeric selectivity inverts from α,α-(1 → 1)-glycosidic bonds for d-glycopyranose acceptors to α,β-(1 → 1)-glycosidic bonds for l-glycopyranose acceptors, while ()-selectivity was retained for both types of sugar acceptors. Comparison of protein crystal structures of trehalose transferase in complex with α,α-trehalose and an unnatural α,β-trehalose analogue highlighted the mechanistic rationale for the observed inversion of anomeric selectivity.

PubMed: 32953231
DOI: 10.1021/acscatal.0c02117

Experimental method

X-RAY DIFFRACTION (2.1 Å)