Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/50360
標題: The crystal structure of a multifunctional protein: Phosphoglucose isomerase autocrine motility factor neuroleukin
作者: Sun, Y.J.
孟孟孝
Chou, C.C.
Chen, W.S.
Wu, R.T.
Meng, M.S.
Hsiao, C.D.
關鍵字: d-xylose isomerase
aldose-ketose interconversion
human
immunodeficiency virus
active-site histidine
glucose-6-phosphate
isomerase
phosphohexose isomerase
bacillus-stearothermophilus
glucosephosphate isomerase
6-phosphoglucose isomerase
crystallographic
structure
期刊/報告no:: Proceedings of the National Academy of Sciences of the United States of America, Volume 96, Issue 10, Page(s) 5412-5417.
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.
URI: http://hdl.handle.net/11455/50360
ISSN: 0027-8424
文章連結: http://dx.doi.org/10.1073/pnas.96.10.5412
Appears in Collections:生物科技學研究所

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