The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 Å resolution
- 1 May 1996
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 3 (5) , 470-479
- https://doi.org/10.1038/nsb0596-470
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 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.Keywords
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