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Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
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Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
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Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
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Journal Article
Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
2020
Overview
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 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X‐ray crystallographic analysis revealed that TlDps1 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. A DNA‐binding protein from starved cells (Dps) protein from nonheterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O‐77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 illustrated that it had higher thermostability than previously reported Dps proteins. X‐ray crystallographic analysis revealed that TlDps1 possessed His‐type ferroxidase centers within the cavity and unique metal‐binding sites located on the surface of the protein.
Publisher
John Wiley & Sons, Inc,John Wiley and Sons Inc,Wiley
Subject
