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5AEE

A bacterial protein structure in glycoside hydrolase family 31

Summary for 5AEE
Entry DOI10.2210/pdb5aee/pdb
Related5AED 5AEG
DescriptorALPHA-GLUCOSIDASE YIHQ, CALCIUM ION, 4-nitrophenyl alpha-D-6-sulfoquinovoside, ... (6 entities in total)
Functional Keywordshydrolase, gh31, alpha-sulfoquinovosidase
Biological sourceESCHERICHIA COLI
Total number of polymer chains2
Total formula weight157850.32
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 citationSpeciale, 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: 26878550
DOI: 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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