The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution.
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.
Cleasby
A
A
Glaxo Wellcome Research and Development, Department of Biomolecular Structure, Stevenage, UK.
Wonacott
A
A
Skarzynski
T
T
Hubbard
R E
RE
Davies
G J
GJ
Proudfoot
A E
AE
Bernard
A R
AR
Payton
M A
MA
Wells
T N
TN
D001665:Binding Sites; D002176:Candida albicans / Q000201:enzymology* / Q000235:genetics; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D008359:Mannose-6-Phosphate Isomerase / Q000737:chemistry* / Q000235:genetics; D008667:Metalloproteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D013045:Species Specificity; D015032:Zinc / Q000737:chemistry*
D008667:Metalloproteins; D011994:Recombinant Proteins; D008359:Mannose-6-Phosphate Isomerase; D015032:Zinc