2PGI

THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE-AN ENZYME WITH AUTOCRINE MOTILITY FACTOR ACTIVITY IN TUMOR CELLS

2PGI の概要

• エントリーDOI: 10.2210/pdb2pgi/pdb
• 分子名称: PHOSPHOGLUCOSE ISOMERASE (2 entities in total)
• 機能のキーワード: phosphoglucose isomerase, autocrinefactor, neuroleukin, motility, glycolysis, isomerase
• 由来する生物種: Geobacillus stearothermophilus
• 細胞内の位置: Cytoplasm: P13376
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50202.76

構造登録者

Sun, Y.-J.,Chou, C.-C.,Chen, W.-S.,Meng, M.,Hsiao, C.-D. (登録日: 1998-10-27, 公開日: 1999-06-15, 最終更新日: 2024-02-21)

主引用文献

Sun, Y.J.,Chou, C.C.,Chen, W.S.,Wu, R.T.,Meng, M.,Hsiao, C.D.
The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin.
Proc.Natl.Acad.Sci.USA, 96:5412-5417, 1999

PubMed Abstract: 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-A 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 alpha/beta 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.

PubMed: 10318897
DOI: 10.1073/pnas.96.10.5412

実験手法

X-RAY DIFFRACTION (2.3 Å)