5aee

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A bacterial protein structure in glycoside hydrolase family 31

Structural highlights

5aee is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:CA, CL, MPD, NSQ
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SQASE_ECOLI Catalyzes the hydrolysis of sulfoquinovosyl diacylglycerides (SQDG) to sulfoquinovose (SQ), which is then degraded by E.coli through the SQ Embden-Meyerhof-Parnas (SQ-EMP) sulfoglycolysis pathway as a source of carbon and sulfur. Therefore, is likely involved in the utilization of the sulfoquinovose headgroup found in ubiquitous plant sulfolipids. Is also able to hydrolyze simple sulfoquinovosides such as 1-sulfoquinovosylglycerol (SQGro). Is a retaining glycoside hydrolase, since it forms the alpha anomer of SQ (PubMed:26878550). Also exhibits some alpha-glucosidase activity against alpha-glucosyl fluoride in vitro, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed (PubMed:15294295).[1] [2]

Publication Abstract from PubMed

Sulfoquinovose is produced by photosynthetic organisms at a rate of 1010 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.

YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids.,Speciale G, Jin Y, Davies GJ, Williams SJ, Goddard-Borger ED Nat Chem Biol. 2016 Feb 15. doi: 10.1038/nchembio.2023. PMID:26878550[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
3 reviews cite this structure
Barton et al. (2017)
No citations found

See Also

References

  1. Okuyama M, Mori H, Chiba S, Kimura A. Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli. Protein Expr Purif. 2004 Sep;37(1):170-9. PMID:15294295 doi:http://dx.doi.org/10.1016/j.pep.2004.05.008
  2. Speciale G, Jin Y, Davies GJ, Williams SJ, Goddard-Borger ED. YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids. Nat Chem Biol. 2016 Feb 15. doi: 10.1038/nchembio.2023. PMID:26878550 doi:http://dx.doi.org/10.1038/nchembio.2023
  3. Speciale G, Jin Y, Davies GJ, Williams SJ, Goddard-Borger ED. YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids. Nat Chem Biol. 2016 Feb 15. doi: 10.1038/nchembio.2023. PMID:26878550 doi:http://dx.doi.org/10.1038/nchembio.2023

Contents


PDB ID 5aee

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