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8X18

Xanthomonas campestris pv. campestris OpgD mutant-D379N with beta-1,2-glucan

Summary for 8X18
Entry DOI10.2210/pdb8x18/pdb
DescriptorGlucans biosynthesis protein D, beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose, beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose-(1-2)-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordstransglycosylase, transferase
Biological sourceXanthomonas campestris pv. campestris str. ATCC 33913
Total number of polymer chains2
Total formula weight129562.20
Authors
Motouchi, S.,Nakajima, M. (deposition date: 2023-11-06, release date: 2024-11-06, Last modification date: 2025-05-28)
Primary citationMotouchi, S.,Komba, S.,Nakai, H.,Nakajima, M.
Discovery of Anomer-Inverting Transglycosylase: Cyclic Glucohexadecaose-Producing Enzyme from Xanthomonas , a Phytopathogen.
J.Am.Chem.Soc., 146:17738-17746, 2024
Cited by
PubMed Abstract: Various species cause well-known plant diseases. Among various pathogenic factors, the role of α-1,6-cyclized β-1,2-glucohexadecaose (CβG16α) produced by pv. was previously shown to be vital for infecting model organisms, and . However, enzymes responsible for biosynthesizing CβG16α are essentially unknown, which limits the generation of agrichemicals that inhibit CβG16α synthesis. In this study, we discovered that OpgD from pv. converts linear β-1,2-glucan to CβG16α. Structural and functional analyses revealed OpgD from pv. possesses an anomer-inverting transglycosylation mechanism, which is unprecedented among glycoside hydrolase family enzymes.
PubMed: 38957137
DOI: 10.1021/jacs.4c02579
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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