9J24

Structural basis of the bifunctionality of M. salinexigens ZYF650T glucosylglycerol phosphorylase in glucosylglycerol catabolism

9J24 の概要

• エントリーDOI: 10.2210/pdb9j24/pdb
• 分子名称: Sucrose phosphorylase, GLYCEROL, alpha-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: glucosylglycerol;phosphorylase-gh13_18;structure-double displacement mechanism, structural protein
• 由来する生物種: Marinobacter salinexigens
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 333096.71

構造登録者

Lu, D.,Ma, H.L. (登録日: 2024-08-06, 公開日: 2025-09-10)

主引用文献

Lu, D.,Zhang, K.,Cheng, C.,Wu, D.,Yin, L.,Luo, Q.,Shi, M.,Ma, H.,Lu, X.
Structural basis of the bifunctionality of Marinobacter salinexigens ZYF650 T glucosylglycerol phosphorylase in glucosylglycerol catabolism.
J.Biol.Chem., 301:108127-108127, 2025

PubMed Abstract: 2-O-α-Glucosylglycerol (GG) is a natural heteroside synthesized by many cyanobacteria and a few heterotrophic bacteria under salt stress conditions. Bacteria produce GG in response to stimuli and degrade it once the stimulus diminishes. Heterotrophic bacteria utilize GG phosphorylase (GGP), a member of the GH13_18 family, via a two-step process consisting of phosphorolysis and hydrolysis for GG catabolism. However, the precise mechanism by which GGP degrades GG remains elusive. We determined the 3D structure of a recently identified GGP (MsGGP) of the deep-sea bacterium Marinobacter salinexigens ZYF650, in complex with glucose and glycerol, α-d-glucose-1-phosphate (αGlc1-P), and orthophosphate (inorganic phosphate) at resolutions of 2.5, 2.7, and 2.7 Å, respectively. Notably, the first αGlc1-P complex structure in the GH13_18 family, the complex of MsGGP and αGlc1-P, validates that GGP catalyzes GG decomposition through consecutive phosphorolysis and hydrolysis. In addition, the structure reveals the mechanism of high stereoselectivity on αGlc1-P. Glu231 and Asp190 were identified as the catalytic residues. Interestingly, these structures closely resemble each other, indicating minimal conformational changes upon binding end-product glucose and glycerol, or the intermediate αGlc1-P. The structures also indicate that the substrates may follow a specific trajectory and a precise order toward the active center in close proximity and in a geometrically favorable orientation for catalysis in a double displacement mechanism.

PubMed: 39725037
DOI: 10.1016/j.jbc.2024.108127

実験手法

X-RAY DIFFRACTION (2.5 Å)