Abstract
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 ˚ 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.
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Cleasby, A., Wonacott, A., Skarzynski, T. et al. The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 Å resolution. Nat Struct Mol Biol 3, 470–479 (1996). https://doi.org/10.1038/nsb0596-470
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DOI: https://doi.org/10.1038/nsb0596-470
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