The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition

被引:50
作者
Chou, CC
Sun, YJ
Meng, MS
Hsiao, CD [1 ]
机构
[1] Acad Sinica, Inst Mol Biol, Taipei 11529, Taiwan
[2] Natl Def Med Ctr, Grad Inst Life Sci, Taipei, Taiwan
[3] Taipei Med Coll, Inst Cell & Mol Biol, Taipei, Taiwan
[4] Natl Chung Hsing Univ, Grad Inst Agr Biotechnol, Taichung 40227, Taiwan
关键词
D O I
10.1074/jbc.M002017200
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
Phosphoglucose isomerase catalyzes the reversible isomerization of glucose 6-phosphate to fructose B-phosphate. In addition, phosphoglucose isomerase has been shown to have functions equivalent to neuroleukin, autocrine motility factor, and maturation factor. Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5- and 2.3-Angstrom resolution, respectively. The inhibitors bind to a region within the domains' interface and interact with a histidine residue (His(306)) from the other subunit. We also demonstrated that the inhibitors not only affect the enzymatic activity of phosphoglucose isomerase, but can also inhibit the autocrine motility factor-induced cell motility of CT-26 mouse colon tumor cells. These results indicate that the substrate and the receptor binding sites of phosphoglucose isomerase and autocrine motility factor are located within close proximity to each other. Based on these two complex structures, together with biological and biochemical results, we propose a possible isomerization mechanism for phosphoglucose isomerase.
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收藏
页码:23154 / 23160
页数:7
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