Open AccessBiochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
Author(s) -
Minato Takuo,
Teramoto Takamasa,
Kakuta Yoshimitsu,
Ogo Seiji,
Yoon KiSeok
Publication year - 2020
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12837
Subject(s) - ceruloplasmin , characterization (materials science) , chemistry , biochemistry , metal , materials science , nanotechnology , organic chemistry
The DNA‐binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from nonheterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic nonheterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O‐77 ( Tl Dps1) was purified and characterized. PAGE and CD analyses of Tl Dps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X‐ray crystallographic analysis revealed that Tl Dps1 possessed His‐type ferroxidase centers within the cavity and unique metal‐binding sites located on the surface of the protein, which presumably contributed to its exceedingly high thermostability.