2f2h | pdb_00002f2h
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| 2f2h, resolution 1.950Å | |||||||||||||
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| Ligands: | SO4, MPO, XTG and GOL | ||||||||||||
| Gene: | yicI (Escherichia coli) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structure of the YicI thiosugar Michaelis complex
Overview
For the first time, the thioglycoligase strategy has been successfully applied to alpha-glycosidases. The alpha-thioglycoligases derived from the family 31 glycosidases, alpha-xylosidase from E. coli (YicI) and alpha-glucosidase from Sulfolobus solfataricus, catalyze thioglycoligase reactions using alpha-glycosyl fluorides and deoxythioglycosides as donors and acceptors, respectively, in yields up to 86%. In addition, we describe the Michaelis complex of YicI using one of the thioglycosides as a nonhydrolyzable substrate analogue and discuss the structural insights this yields into the specificity and mechanism of family 31 alpha-glycosidases and the molecular basis of an associated genetic disease.
About this Structure
2F2H is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Expanding the thioglycoligase strategy to the synthesis of alpha-linked thioglycosides allows structural investigation of the parent enzyme/substrate complex., Kim YW, Lovering AL, Chen H, Kantner T, McIntosh LP, Strynadka NC, Withers SG, J Am Chem Soc. 2006 Feb 22;128(7):2202-3. PMID:16478160
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