8X18
Xanthomonas campestris pv. campestris OpgD mutant-D379N with beta-1,2-glucan
Summary for 8X18
| Entry DOI | 10.2210/pdb8x18/pdb |
| Descriptor | Glucans 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 Keywords | transglycosylase, transferase |
| Biological source | Xanthomonas campestris pv. campestris str. ATCC 33913 |
| Total number of polymer chains | 2 |
| Total formula weight | 129562.20 |
| Authors | Motouchi, S.,Nakajima, M. (deposition date: 2023-11-06, release date: 2024-11-06, Last modification date: 2025-05-28) |
| Primary citation | Motouchi, 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: 38957137DOI: 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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