Weerth R Sophia, Michalska Karolina, Bingman Craig A, Yennamalli Ragothaman M, Li Hui, Jedrzejczak Robert, Wang Fengbin, Babnigg Gyorgy, Joachimiak Andrzej, Thomas Michael G, Phillips George N
Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin.
Proteins. 2015 Feb;83(2):383-8. doi: 10.1002/prot.24705. Epub 2014 Dec 18.
Proteins belonging to the cupin superfamily have a wide range of catalytic and noncatalytic functions. Cupin proteins commonly have the capacity to bind a metal ion with the metal frequently determining the function of the protein. We have been investigating the function of homologous cupin proteins that are conserved in more than 40 species of bacteria. To gain insights into the potential function of these proteins we have solved the structure of Plu4264 from Photorhabdus luminescens TTO1 at a resolution of 1.35 Å and identified manganese as the likely natural metal ligand of the protein.
属于cupin超家族的蛋白质具有广泛的催化和非催化功能。Cupin蛋白通常具有结合金属离子的能力，金属常常决定了蛋白质的功能。我们一直在研究在40多种细菌中保守的同源cupin蛋白的功能。为了深入了解这些蛋白质的潜在功能，我们已解析了来自发光光杆状菌TTO1的Plu4264的结构，分辨率为1.35 Å，并确定锰是该蛋白质可能的天然金属配体。
