The crystal structure of a multifunctional protein: Phosphoglucose isomerase autocrine motility factor neuroleukin

被引：102

作者：

Sun, YJ

Chou, CC

Chen, WS

Wu, RT

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 11217, Taiwan

[3] Vet Gen Hosp, Taipei 11221, Taiwan

[4] Natl Yang Ming Univ, Grad Inst Biopharmaceut Sci, Riyadh 11211, Saudi Arabia

[5] Natl Chung Hsing Univ, Grad Inst Agr Biotechnol, Taichung 40227, Taiwan

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 10期

关键词：

D O I：

10.1073/pnas.96.10.5412

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3-Angstrom resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted alp structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.

引用

页码：5412 / 5417

页数：6

共 65 条

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