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

研究成果: Contribution to journalArticle

抜粋

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.

元の言語英語
ページ(範囲)1219-1229
ページ数11
ジャーナルFEBS Open Bio
10
発行部数7
DOI
出版物ステータス出版済み - 7 1 2020

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

フィンガープリント Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

  • これを引用