6LKP

Crystal structure of Dps1 from the thermophilic non-heterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O-77

Summary for 6LKP

• Entry DOI: 10.2210/pdb6lkp/pdb
• Descriptor: DNA protection during starvation protein, ZINC ION, FE (III) ION (3 entities in total)
• Functional Keywords: the dna-binding protein from starved cells, dps, ferritin superfamily, dodecamer, dna binding protein
• Biological source: Leptolyngbya sp. O-77
• Total number of polymer chains: 6
• Total formula weight: 125482.29

Authors

Minato, T.,Teramoto, T.,Kakuta, Y.,Ogo, S.,Yoon, K.S. (deposition date: 2019-12-19, release date: 2020-03-25, Last modification date: 2023-11-22)

Primary citation

Minato, T.,Teramoto, T.,Kakuta, Y.,Ogo, S.,Yoon, K.S.
Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites.
Febs Open Bio, 10:1219-1229, 2020

PubMed 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.

PubMed: 32170832
DOI: 10.1002/2211-5463.12837

Experimental method

X-RAY DIFFRACTION (2.9 Å)