7N6O
The crystal structure of the GH30 subfamily 10 enzyme, AcXbh30A from Acetivibrio clariflavus in complex with xylobiose
Summary for 7N6O
| Entry DOI | 10.2210/pdb7n6o/pdb |
| Related | 7N6H |
| Related PRD ID | PRD_900116 |
| Descriptor | AcXbh30A, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | gh30, hydrolase |
| Biological source | Acetivibrio clariflavus |
| Total number of polymer chains | 2 |
| Total formula weight | 101111.32 |
| Authors | Tan, K.,St John, J.F. (deposition date: 2021-06-08, release date: 2022-08-17, Last modification date: 2023-10-18) |
| Primary citation | St John, F.J.,Crooks, C.,Kim, Y.,Tan, K.,Joachimiak, A. The first crystal structure of a xylobiose-bound xylobiohydrolase with high functional specificity from the bacterial glycoside hydrolase family 30, subfamily 10. Febs Lett., 596:2449-2464, 2022 Cited by PubMed Abstract: Xylobiose is a prebiotic sugar that has applications in functional foods. This report describes the first X-ray crystallographic structure models of apo and xylobiose-bound forms of a xylobiohydrolase (XBH) from Acetivibrio clariflavus. This xylan-active enzyme, a member of the recently described glycoside hydrolase family 30 (GH30), subfamily 10, phylogenetic clade has been shown to strictly release xylobiose as its primary hydrolysis product. Inspection of the apo structure reveals a glycone region X -binding slot. When X binds, the non-reducing xylose in the -2 subsite is highly coordinated with numerous hydrogen bond contacts while contacts in the -1 subsite mostly reflect interactions typical for GH30 and enzymes in clan A of the carbohydrate-active enzymes database (CAZy). This structure provides an explanation for the high functional specificity of this new bacterial GH30 XBH subfamily. PubMed: 35876256DOI: 10.1002/1873-3468.14454 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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