7WCG

Single-Stranded DNA binding protein of Sulfolobus Solfataricus structure at high-temperature

Summary for 7WCG

• Entry DOI: 10.2210/pdb7wcg/pdb
• Descriptor: Single-stranded DNA binding protein Ssb (1 entity in total)
• Functional Keywords: ob-fold, hyperthermophilic, structure at high-temperature, dna binding protein
• Biological source: Saccharolobus solfataricus P2
• Total number of polymer chains: 1
• Total formula weight: 14162.73

Authors

Yang, M.J.,Park, C.,Lee, W. (deposition date: 2021-12-20, release date: 2022-06-08, Last modification date: 2024-05-15)

Primary citation

Yang, M.J.,Kim, J.,Lee, Y.,Lee, W.,Park, C.J.
NMR Structure and Biophysical Characterization of Thermophilic Single-Stranded DNA Binding Protein from Sulfolobus Solfataricus .
Int J Mol Sci, 23:-, 2022

PubMed Abstract: Proteins from , an extremophile, are active even at high temperatures. The single-stranded DNA (ssDNA) binding protein of (SsoSSB) is overexpressed to protect ssDNA during DNA metabolism. Although SsoSSB has the potential to be applied in various areas, its structural and ssDNA binding properties at high temperatures have not been studied. We present the solution structure, backbone dynamics, and ssDNA binding properties of SsoSSB at 50 °C. The overall structure is consistent with the structures previously studied at room temperature. However, the loop between the first two β sheets, which is flexible and is expected to undergo conformational change upon ssDNA binding, shows a difference from the ssDNA bound structure. The ssDNA binding ability was maintained at high temperature, but different interactions were observed depending on the temperature. Backbone dynamics at high temperature showed that the rigidity of the structured region was well maintained. The investigation of an N-terminal deletion mutant revealed that it is important for maintaining thermostability, structure, and ssDNA binding ability. The structural and dynamic properties of SsoSSB observed at high temperature can provide information on the behavior of proteins in thermophiles at the molecular level and guide the development of new experimental techniques.

PubMed: 35328522
DOI: 10.3390/ijms23063099

Experimental method

SOLUTION NMR