7MSK

ThuS glycosin S-glycosyltransferase

Summary for 7MSK

• Entry DOI: 10.2210/pdb7msk/pdb
• Descriptor: Glyco_trans_2-like domain-containing protein, MAGNESIUM ION, URIDINE-5'-DIPHOSPHATE-2-DEOXY-2-FLUORO-ALPHA-D-GLUCOSE, ... (4 entities in total)
• Functional Keywords: glycosin, ripp, glycosyltransferase, biosynthetic protein
• Biological source: Bacillus thuringiensis serovar andalousiensis BGSC 4AW1
• Total number of polymer chains: 2
• Total formula weight: 102094.12

Authors

Garg, N.,Nair, S.K. (deposition date: 2021-05-11, release date: 2022-04-13, Last modification date: 2024-05-22)

Primary citation

Fujinami, D.,Garcia de Gonzalo, C.V.,Biswas, S.,Hao, Y.,Wang, H.,Garg, N.,Lukk, T.,Nair, S.K.,van der Donk, W.A.
Structural and mechanistic investigations of protein S-glycosyltransferases.
Cell Chem Biol, 28:1740-1749.e6, 2021

PubMed Abstract: Attachment of sugars to nitrogen and oxygen in peptides is ubiquitous in biology, but glycosylation of sulfur atoms has only been recently described. Here, we characterize two S-glycosyltransferases SunS and ThuS that selectively glycosylate one of five Cys residues in their substrate peptides; substitution of this Cys with Ser results in a strong decrease in glycosylation activity. Crystal structures of SunS and ThuS in complex with UDP-glucose or a derivative reveal an unusual architecture in which a glycosyltransferase type A (GTA) fold is decorated with additional domains to support homodimerization. Dimer formation creates an extended cavity for the substrate peptide, drawing functional analogy with O-glycosyltransferases involved in cell wall biosynthesis. This extended cavity contains a sharp bend that may explain the site selectivity of the glycosylation because the target Cys is in a Gly-rich stretch that can accommodate the bend. These studies establish a molecular framework for understanding the unusual S-glycosyltransferases.

PubMed: 34283964
DOI: 10.1016/j.chembiol.2021.06.009

Experimental method

X-RAY DIFFRACTION (2.06 Å)