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Nat Struct Biol. 1996 May;3(5):470-9.

The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution.

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Glaxo Wellcome Research and Development, Department of Biomolecular Structure, Stevenage, UK.


Phosphomannose isomerase (PMI) catalyses the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P). Absence of PMI activity in yeasts causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs. The 1.7 A crystal structure of PMI from Candida albicans shows that the enzyme has three distinct domains. The active site lies in the central domain, contains a single essential zinc atom, and forms a deep, open cavity of suitable dimensions to contain M6P or F6P The central domain is flanked by a helical domain on one side and a jelly-roll like domain on the other.

[Indexed for MEDLINE]

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