The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution
The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution
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DOI：
10.1038/nsb0596-470
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发表时间：
1996-05-01
期刊：
影响因子：
--
通讯作者：
Wells, TNC
中科院分区：
文献类型：
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作者：
Cleasby, A;Wonacott, A;Wells, TNC
磷酸甘露糖异构酶(PMI)催化6-磷酸果糖(F6P)和6-磷酸甘露糖(M6P)的可逆异构化。酵母中缺乏PMI活性会导致细胞裂解，因此该酶是一个潜在的抑制目标，并可能成为抗真菌药物的一条途径。白色念珠菌PMI的1.7埃晶体结构表明，该酶有三个不同的结构域。活性部位位于中心区域，包含一个单一的必需锌原子，并形成一个深的、开放的空腔，尺寸合适，以包含M6P或F6P。中心结构域的一侧是螺旋状结构域，另一侧是果冻卷状结构域。
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.