Structural highlights
Publication Abstract from PubMed
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 non-heterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic non-heterocystous 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.
Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites.,Minato T, Teramoto T, Kakuta Y, Ogo S, Yoon KS FEBS Open Bio. 2020 Mar 14. doi: 10.1002/2211-5463.12837. PMID:32170832[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Minato T, Teramoto T, Kakuta Y, Ogo S, Yoon KS. Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites. FEBS Open Bio. 2020 Mar 14. doi: 10.1002/2211-5463.12837. PMID:32170832 doi:http://dx.doi.org/10.1002/2211-5463.12837
