6rqk
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Crystal structure of GH125 1,6-alpha-mannosidase from Clostridium perfringens in complex with mannoimidazole
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Structural highlights
FunctionPublication Abstract from PubMedEnzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Here, mannoimidazole, a mimic of the transition state of mannosidase catalyzed hydrolysis of mannosides, is shown to bind in a B2,5 conformation on the Clostridium perfringens GH125 alpha-1,6-mannosidase, providing additional evidence of a OS2-B2,5-1S5 conformational itinerary for enzymes of this family. Distortion of mannoimidazole supports a B2,5 boat transition state for the family GH125 alpha-1,6-mannosidase from Clostridium perfringens.,Males A, Speciale G, Williams SJ, Davies GJ Org Biomol Chem. 2019 Aug 13. doi: 10.1039/c9ob01161g. PMID:31407758[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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