Dps-like proteins: structural and functional insights into a versatile protein family

被引:117
作者
Haikarainen, Teemu [1 ,2 ]
Papageorgiou, Anastassios C. [1 ,2 ]
机构
[1] Univ Turku, Turku Ctr Biotechnol, Turku 20521, Finland
[2] Abo Akad Univ, Turku 20521, Finland
关键词
Oxidative stress; Mini-ferritins; Metal binding; Ferroxidase; Fenton reaction; Iron binding; Zinc; NEUTROPHIL-ACTIVATING PROTEIN; IRON-BINDING PROTEIN; ESCHERICHIA-COLI DPS; OXIDATIVE STRESS RESISTANCE; MYCOBACTERIUM-SMEGMATIS DPS; HYDROGEN-PEROXIDE STRESS; HELICOBACTER-PYLORI; DNA-BINDING; CRYSTAL-STRUCTURE; FERROXIDASE CENTER;
D O I
10.1007/s00018-009-0168-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Dps-like proteins are key factors involved in the protection of prokaryotic cells from oxidative damage. They act by either oxidizing iron to prevent the formation of oxidative radicals or by forming Dps-DNA complexes to physically protect DNA. All Dps-like proteins are characterized by a common three-dimensional architecture and are found as spherical dodecamers with a hollow central cavity. Despite their structural similarities, recent biochemical and structural data have suggested different functions among members of the family that range from protection inside the cells in response to various stress signals to adhesion and virulence during bacterial infections. Moreover, the Dps-like proteins have lately attracted considerable interest in the field of nanotechnology owing to their ability to act as protein cages for iron and various other metals. A better understanding of their function and mechanism could therefore lead to novel applications in biotechnology and nanotechnology.
引用
收藏
页码:341 / 351
页数:11
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