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

Structural highlights

7wcg is a 1 chain structure with sequence from Saccharolobus solfataricus P2. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SSB_SACS2 Binds to ssDNA, binding approximately 5 nucleotides per monomer. Binding my be slightly cooperative. Inhibits the endonuclease activity of XPF.[1]

Publication Abstract from PubMed

Proteins from Sulfolobus solfataricus (S. solfataricus), an extremophile, are active even at high temperatures. The single-stranded DNA (ssDNA) binding protein of S. solfataricus (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 degrees C. The overall structure is consistent with the structures previously studied at room temperature. However, the loop between the first two beta 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.

NMR Structure and Biophysical Characterization of Thermophilic Single-Stranded DNA Binding Protein from Sulfolobus Solfataricus.,Yang MJ, Kim J, Lee Y, Lee W, Park CJ Int J Mol Sci. 2022 Mar 13;23(6). pii: ijms23063099. doi: 10.3390/ijms23063099. PMID:35328522[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Roberts JA, Bell SD, White MF. An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA. Mol Microbiol. 2003 Apr;48(2):361-71. doi: 10.1046/j.1365-2958.2003.03444.x. PMID:12675797 doi:http://dx.doi.org/10.1046/j.1365-2958.2003.03444.x
  2. Yang MJ, Kim J, Lee Y, Lee W, Park CJ. NMR Structure and Biophysical Characterization of Thermophilic Single-Stranded DNA Binding Protein from Sulfolobus Solfataricus. Int J Mol Sci. 2022 Mar 13;23(6). pii: ijms23063099. doi: 10.3390/ijms23063099. PMID:35328522 doi:http://dx.doi.org/10.3390/ijms23063099
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