Studies on molecular structure of metalloproteins

2014 Fiscal Year Final Research Report

• Project/Area Number: 24570163
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Functional biochemistry
• Research Institution: Ehime University
• Principal Investigator: SUGIURA Miwa 愛媛大学, プロテオサイエンスセンター, 准教授 (80312255)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 金属タンパク質

Outline of Final Research Achievements

Zinc ion is an essential element acting as a cofactor in more than 300 enzymes. However, high concentrations of Zn2+ are lethal for the cells. Thermophilic cyanobacterium, Thermosynechococcus elongatus, revealed higher resistance for Zn and Cd compared to other bacteria. In this study, we found that heavy-metal binding protein, metallothionein, in T. elongatus makes pentamer binding 50 atoms of Zn2+. Thus formation of multimer bound many Zn must be the reason of resistance to high concentration of Zn. Furthermore, we tried to analyse the molecular structure of this metallothionein by X-ray crystal structure. Although we obtained many crystals, the resolution was not high enough to know the molecular structure. Now, we are still working on cristallization for better resolution.

Free Research Field

生物物理