5OHY
A GH31 family sulfoquinovosidase in complex with aza-sugar inhibitor IFGSQ
Summary for 5OHY
| Entry DOI | 10.2210/pdb5ohy/pdb |
| Descriptor | Alpha-glucosidase yihQ, POTASSIUM ION, 1,2-ETHANEDIOL, ... (7 entities in total) |
| Functional Keywords | sulfoglycosidase, sulfoglycolysis, complex, general acid-base varient, hydrolase |
| Biological source | Agrobacterium tumefaciens |
| Total number of polymer chains | 4 |
| Total formula weight | 303126.99 |
| Authors | Jin, Y.,Williams, S.J.,Goddard-Borger, E.,Davies, G.J. (deposition date: 2017-07-18, release date: 2018-08-08, Last modification date: 2024-05-01) |
| Primary citation | Abayakoon, P.,Jin, Y.,Lingford, J.P.,Petricevic, M.,John, A.,Ryan, E.,Wai-Ying Mui, J.,Pires, D.E.V.,Ascher, D.B.,Davies, G.J.,Goddard-Borger, E.D.,Williams, S.J. Structural and Biochemical Insights into the Function and Evolution of Sulfoquinovosidases. ACS Cent Sci, 4:1266-1273, 2018 Cited by PubMed Abstract: An estimated 10 billion tonnes of sulfoquinovose (SQ) are produced and degraded each year. Prokaryotic sulfoglycolytic pathways catabolize sulfoquinovose (SQ) liberated from plant sulfolipid, or its delipidated form α-d-sulfoquinovosyl glycerol (SQGro), through the action of a sulfoquinovosidase (SQase), but little is known about the capacity of SQ glycosides to support growth. Structural studies of the first reported SQase ( YihQ) have identified three conserved residues that are essential for substrate recognition, but crossover mutations exploring active-site residues of predicted SQases from other organisms have yielded inactive mutants casting doubt on bioinformatic functional assignment. Here, we show that SQGro can support the growth of on par with d-glucose, and that the SQase prefers the naturally occurring diastereomer of SQGro. A predicted, but divergent, SQase from proved to have highly specific activity toward SQ glycosides, and structural, mutagenic, and bioinformatic analyses revealed the molecular coevolution of catalytically important amino acid pairs directly involved in substrate recognition, as well as structurally important pairs distal to the active site. Understanding the defining features of SQases empowers bioinformatic approaches for mapping sulfur metabolism in diverse microbial communities and sheds light on this poorly understood arm of the biosulfur cycle. PubMed: 30276262DOI: 10.1021/acscentsci.8b00453 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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