1PMI

Candida Albicans Phosphomannose Isomerase

1PMI の概要

• エントリーDOI: 10.2210/pdb1pmi/pdb
• 分子名称: PHOSPHOMANNOSE ISOMERASE, ZINC ION (3 entities in total)
• 機能のキーワード: aldose-ketose isomerase, isomerase
• 由来する生物種: Candida albicans
• 細胞内の位置: Cytoplasm (Probable): P34948
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48855.58

構造登録者

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. (登録日: 1996-04-03, 公開日: 1997-03-01, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)