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

A Cleasby, A Wonacott, T Skarzynski, R E Hubbard, G J Davies, A E I Proudfoot, A R Bernard, M A Payton, T N C Wells

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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 Angstrom 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.

Original languageEnglish
Pages (from-to)470-479
Number of pages10
JournalNature Structural Biology
Issue number5
Publication statusPublished - May 1996



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