9j25

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

spinqualitylabelsall models 9j25, resolution 2.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9j25 is a 3 chain structure with sequence from Marinobacter salinexigens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.74Å Ligands: PEG, PO4, SO4, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A5B0VBK8_9GAMM Publication Abstract from PubMed 2-O-alpha-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(T), in complex with glucose and glycerol, alpha-d-glucose-1-phosphate (alphaGlc1-P), and orthophosphate (inorganic phosphate) at resolutions of 2.5, 2.7, and 2.7 A, respectively. Notably, the first alphaGlc1-P complex structure in the GH13_18 family, the complex of MsGGP and alphaGlc1-P, validates that GGP catalyzes GG decomposition through consecutive phosphorolysis and hydrolysis. In addition, the structure reveals the mechanism of high stereoselectivity on alphaGlc1-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 alphaGlc1-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. Structural basis of the bifunctionality of Marinobacter salinexigens ZYF650(T) glucosylglycerol phosphorylase in glucosylglycerol catabolism.,Lu D, Zhang K, Cheng C, Wu D, Yin L, Luo Q, Shi M, Ma H, Lu X J Biol Chem. 2025 Feb;301(2):108127. doi: 10.1016/j.jbc.2024.108127. Epub 2024 , Dec 25. PMID:39725037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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