The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution

被引：104
作者：
Cleasby, A
Wonacott, A
Skarzynski, T
Hubbard, RE
Davies, GJ
Proudfoot, AEI
Bernard, AR
Payton, MA
Wells, TNC
机构：
[1] UNIV YORK, DEPT CHEM, YORK YO1 5DD, N YORKSHIRE, ENGLAND
[2] GLAXO INST MOLEC BIOL SA, CH-1228 PLAN LES OUATES, GENEVA, SWITZERLAND
来源：
NATURE STRUCTURAL BIOLOGY | 1996年 / 3卷 / 05期
关键词：
D O I：
10.1038/nsb0596-470
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 Angstrom 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.
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收藏
页码：470 / 479
页数：10
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