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A stabilizing alpha/beta-hydrophobic core greatly contributes to hyperthermostability of archaeal [P62A]Ssh10b.

Fang X, Cui Q, Tong Y, Feng Y, Shan L, Huang L, Wang J
Biochemistry 47 11212-21 (2008)
Cited: 9 times
EuropePMC logo PMID: 18821773

Abstract

The hyperthermophilic Ssh10b from Sulfolobus shibatae is a member of the Sac10b family, which has been postulated to play a role in chromosomal organization in Archaea. Ssh10b is capable of significantly constraining negative DNA supercoils at elevated temperatures. In this study, the solution structure of the dimeric P62A mutant Ssh10b ([P62A]Ssh10b) was determined by multidimensional NMR spectroscopy. The backbone 15N dynamics, H/D exchange with and without the denaturant GdmSCN, and chemical and thermal denaturation experiments were performed to investigate the molecular basis of high thermostability of [P62A]Ssh10b. Data analysis has revealed an alpha/beta-hydrophobic core consisting of two alpha-helices and one beta-sheet which are stabilized by cooperative hydrophobic and hydrogen-bonding interactions. This stabilizing alpha/beta-hydrophobic core of [P62A]Ssh10b exhibiting highly restricted internal motions is composed of residues having highly protected amide protons which exchange with solvent mostly by means of a global unfolding process. The K40N mutation greatly destabilizes the mutant [P62A]Ssh10b because this mutation disturbs the packing of alpha-helix against the beta-sheet reducing the stability of the alpha/beta-hydrophobic core in the mutant protein. In comparison with homologous mesophilic and thermophilic proteins, it can be presumed that the stabilizing alpha/beta-hydrophobic core in the [P62A]Ssh10b structure greatly contributes to the high thermostability of the protein.

Articles citing this publication (9)

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  3. Structural Characterization of an ACP from Thermotoga maritima: Insights into Hyperthermal Adaptation. Lee Y, Jang A, Jeong MC, Park N, Park J, Lee WC, Cheong C, Kim Y. Int J Mol Sci 21 E2600 (2020)
  4. Mth10b, a unique member of the Sac10b family, does not bind nucleic acid. Liu YF, Zhang N, Yao HW, Yao HW, Pan XM, Ge M. PLoS One 6 e19977 (2011)
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  6. 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 23 3099 (2022)
  7. Alba from Thermoplasma volcanium belongs to α-NAT's: An insight into the structural aspects of Tv Alba and its acetylation by Tv Ard1. Ma C, Pathak C, Lee SJ, Lee KY, Jang SB, Nam M, Im H, Yoon HJ, Lee BJ. Arch Biochem Biophys 590 90-100 (2016)
  8. Solution structure and calcium binding of protein SSO6904 from the hyperthermophilic archaeon Sulfolobus solfataricus. Feng Y, Yao H, Yao H, Wang J. Proteins 78 474-479 (2010)
  9. Exploring the influence of hyperthermophilic protein Ssh10b on the stability and conformation of RNA by molecular dynamics simulation. Zhang X, Zheng QC. Biopolymers 109 (2018)


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