5AEE
A bacterial protein structure in glycoside hydrolase family 31
Summary for 5AEE
| Entry DOI | 10.2210/pdb5aee/pdb |
| Related | 5AED 5AEG |
| Descriptor | ALPHA-GLUCOSIDASE YIHQ, CALCIUM ION, 4-nitrophenyl alpha-D-6-sulfoquinovoside, ... (6 entities in total) |
| Functional Keywords | hydrolase, gh31, alpha-sulfoquinovosidase |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 2 |
| Total formula weight | 157850.32 |
| Authors | Jin, Y.,Speciale, G.,Davies, G.J.,Williams, S.J.,Goddard-Borger, E.D. (deposition date: 2015-08-28, release date: 2016-02-10, Last modification date: 2024-01-10) |
| Primary citation | Speciale, G.,Jin, Y.,Davies, G.J.,Williams, S.J.,Goddard-Borger, E.D. Yihq is a Sulfoquinovosidase that Cleaves Sulfoquinovosyl Diacylglyceride Sulfolipids. Nat.Chem.Biol., 12:215-, 2016 Cited by PubMed Abstract: Sulfoquinovose is produced by photosynthetic organisms at a rate of 10(10) tons per annum and is degraded by bacteria as a source of carbon and sulfur. We have identified Escherichia coli YihQ as the first dedicated sulfoquinovosidase and the gateway enzyme to sulfoglycolytic pathways. Structural and mutagenesis studies unveiled the sequence signatures for binding the distinguishing sulfonate residue and revealed that sulfoquinovoside degradation is widespread across the tree of life. PubMed: 26878550DOI: 10.1038/NCHEMBIO.2023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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