1PMI

Candida Albicans Phosphomannose Isomerase

Summary for 1PMI

• Entry DOI: 10.2210/pdb1pmi/pdb
• Descriptor: PHOSPHOMANNOSE ISOMERASE, ZINC ION (3 entities in total)
• Functional Keywords: aldose-ketose isomerase, isomerase
• Biological source: Candida albicans
• Cellular location: Cytoplasm (Probable): P34948
• Total number of polymer chains: 1
• Total formula weight: 48855.58

Authors

Cleasby, A.,Skarzynski, T.,Wonacott, A.,Davies, G.J.,Hubbard, R.E.,Proudfoot, A.E.I.,Wells, T.N.C.,Payton, M.A.,Bernard, A.R. (deposition date: 1996-04-03, release date: 1997-03-01, Last modification date: 2024-02-14)

Primary citation

Cleasby, A.,Wonacott, A.,Skarzynski, T.,Hubbard, R.E.,Davies, G.J.,Proudfoot, A.E.,Bernard, A.R.,Payton, M.A.,Wells, T.N.
The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution.
Nat.Struct.Biol., 3:470-479, 1996

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.

PubMed: 8612079
DOI: 10.1038/nsb0596-470

Experimental method

X-RAY DIFFRACTION (1.7 Å)