Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)1219-1229
Number of pages11
JournalFEBS Open Bio
Volume10
Issue number7
DOIs
Publication statusPublished - Jul 1 2020

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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