Tsinghua Professors Wu Jia-Wei and Shi Yigong Publish Papers in Nature and Science respectively

By Li Han
Staff Writer of the Tsinghua News Center

Tsinghua University Professor Wu Jia-Wei published a paper in Nature
(advanced on line 2009 May 27), entitled “Structural insight into the
autoinhibition mechanism of AMP-activated protein kinase”. The group led by
Professor Shi Yigong at Tsinghua University published their recent research
findings in Science (advanced on line 2009 May 28), entitled “Structure and
mechanism of an amino acid antiporter”.

Professor Wu and her group reported the crystal structures of an
unphosphorylated AMPK (AMP-activated protein kinase) fragment that contains
a catalytic kinase domain and an autoinhibitory domain (AID), and of a
phosphorylated kinase domain. The structural analyses and in vitro kinetic
studies demonstrate the autoinhibition mechanism of AMPK. In this article,
the structural and biochemical data have shown how the primary mechanism of
AMPK autoinhibition works and suggest a conformational switch model for AMPK
activation by AMP. These results may lay a theoretical foundation for the
new drug discovery in therapy of type 2 diabetes.

Professor Shi Yigong’s team reported the crystal structure of Adic, an
arginine-agmatine antiporter that plays essential role in the
acid-resistance system of virulent enteric pathogens. Structural and
biochemical analyses revealed the potential ligand-binding sites, and the
transport route. Their study suggested a conserved mechanism for the
antiporter activity. This is the first crystal structure of the membrane
protein in the amino acid/polyamine/organocation (APC) transporter
superfamily, a class of transporters that consist of more than 250 members,
conserved from bacteria to human being. The reported structure will shed
light on the further understanding of APC proteins in prokaryotes and
eukaryotes.

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