Nature Structural Biology
3, 470 - 479 (1996)
doi:10.1038/nsb0596-470
The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 Å resolutionAnne Cleasby1, Alan Wonacott1, Tadeusz Skarzynski1, Roderick E. Hubbard2, Gideon J. Davies2, Amanda E. I. Proudfoot3, Alain R. Bernard3, Mark A. Payton3
& Timothy N.C. Wells3
1Glaxo Wellcome Research and Development Department of Biomolecular Structure, Glaxo Wellcome Medicines Research Centre, Gunnels Wood Road, Stevenage, SG1 2NY, UK
2Department of Chemistry, University of York, Heslington, York,Y01 5DD, UK
3Glaxo Institute of Molecular Biology, 1228 Plan-les-Ouates, Geneva, Switzerland 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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