7XPU

crystal structure of MtdL-S228A-His soaked GDP-Fucp and Mn

Summary for 7XPU

• Entry DOI: 10.2210/pdb7xpu/pdb
• Descriptor: Transglycosylse, GUANOSINE-5'-DIPHOSPHATE-BETA-L-FUCOPYRANOSE, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: transferase
• Biological source: Marinactinospora thermotolerans
• Total number of polymer chains: 2
• Total formula weight: 89104.72

Authors

Li, F.D.,He, C. (deposition date: 2022-05-05, release date: 2023-03-29, Last modification date: 2023-11-29)

Primary citation

Du, X.,Chu, X.,Liu, N.,Jia, X.,Peng, H.,Xiao, Y.,Liu, L.,Yu, H.,Li, F.,He, C.
Structures of the NDP-pyranose mutase belonging to glycosyltransferase family 75 reveal residues important for Mn 2+ coordination and substrate binding.
J.Biol.Chem., 299:102903-102903, 2023

PubMed Abstract: Members of glycosyltransferase family 75 (GT75) not only reversibly catalyze the autoglycosylation of a conserved arginine residue with specific NDP-sugars but also exhibit NDP-pyranose mutase activity that reversibly converts specific NDP-pyranose to NDP-furanose. The latter activity provides valuable NDP-furanosyl donors for glycosyltransferases and requires a divalent cation as a cofactor instead of FAD used by UDP-D-galactopyranose mutase. However, details of the mechanism for NDP-pyranose mutase activity are not clear. Here we report the first crystal structures of GT75 family NDP-pyranose mutases. The novel structures of GT75 member MtdL in complex with Mn and GDP, GDP-D-glucopyranose, GDP-L-fucopyranose, GDP-L-fucofuranose, respectively, combined with site-directed mutagenesis studies, reveal key residues involved in Mn coordination, substrate binding, and catalytic reactions. We also provide a possible catalytic mechanism for this unique type of NDP-pyranose mutase. Taken together, our results highlight key elements of an enzyme family important for furanose biosynthesis.

PubMed: 36642179
DOI: 10.1016/j.jbc.2023.102903

Experimental method

X-RAY DIFFRACTION (2.2 Å)