Work

Structural analysis of the tetrahydrobiopterin glucosyltransferase Ps BGluT from Pseudanabaena sp. Chao 1811

Year: 2025

Type: article

Abstract: Pterin glycosides are widely distributed in cyanobacteria and have been implicated in the regulation of phototaxis and photosynthesis. Here, we identified a new uridine diphosphate glucose:tetrahydrobiopterin α-glucosyltransferase, termed Ps BGluT, from Pseudanabaena sp. Chao 1811, which catalyzes the formation of pterin glycosides. We solved crystal structures of apo Ps BGluT and its UDP-bound form at 2.8 and 2.3 Å resolution, respectively. Ps BGluT forms a homodimer, with each subunit adopting a canonical GT-B fold composed of two Rossmann-like domains. Structural analysis combined with molecular docking revealed the binding sites for both the donor UDP-glucose and the acceptor tetrahydrobiopterin. Based on these findings, we proposed that Ps BGluT operates via an S N i retaining catalytic mechanism. This study advances our understanding of pteridine glycosylation and also provides a structural basis for investigating the photosynthetic signaling pathways in cyanobacteria.

Source: Acta Crystallographica Section F Structural Biology Communications

DOI: 10.1107/s2053230x25009446

Authors: Ruijie Zang, Yongliang Jiang, Cong-Zhao Zhou

Institution: University of Science and Technology of China

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

Funder: National Natural Science Foundation of China

Award: G5697829477