| Literature DB >> 8612079 |
A Cleasby1, A Wonacott, T Skarzynski, R E Hubbard, G J Davies, A E Proudfoot, A R Bernard, M A Payton, T N Wells.
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.Entities:
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Year: 1996 PMID： 8612079 DOI： 10.1038/nsb0596-470
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368