Download MendeleyThe x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution.
Cleasby, A., Wonacott, A., Skarzynski, T., Hubbard, R.E., Davies, G.J., Proudfoot, A.E., Bernard, A.R., Payton, M.A., Wells, T.N.(1996) Nat Struct Biol 3: 470-479
- PubMed: 8612079
- DOI: https://doi.org/10.1038/nsb0596-470
- Primary Citation of Related Structures:
1PMI - PubMed 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.
Organizational Affiliation:
Glaxo Wellcome Research and Development, Department of Biomolecular Structure, Stevenage, UK.
