An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility

Michael A. Durney, Rainer W. Wechselberger, Charalampos G. Kalodimos, Robert Kaptein, Constantinos E. Vorgias, Rolf Boelens

Research output: Contribution to journalArticle

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Abstract

The homodimeric HU protein from the hyperthermophile Thermotoga maritima (HUTmar) is a model system which can yield insights into the molecular determinants of thermostability in proteins. Unusually for a thermostable protein, HUTmar exists in a structurally heterogeneous state as evidenced by the assignment of two distinct and approximately equally populated forms in solution. Relaxation measurements combined with chemical shift, hydrogen exchange, and nuclear Overhauser enhancement data confirm the main structural features of both forms. In addition, these data support a two-state model for HUTmar in which the major form closely resembles the X-ray structure while the very flexible minor form is less structured. HUTmar may therefore be a new example of the small class of hyperthermostable proteins with unexpected flexibility.

Original languageEnglish (US)
Pages (from-to)49-54
Number of pages6
JournalFEBS Letters
Volume563
Issue number1-3
DOIs
StatePublished - Apr 9 2004

Keywords

  • Conformational flexibility
  • HUBst, Bacillus stearothermophilus HU protein
  • HUBsu, Bacillus subtilis HU protein
  • HUTmar, Thermotoga maritima HU protein
  • Nuclear magnetic resonance spin relaxation
  • Protein dynamics
  • Thermostability

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    Durney, M. A., Wechselberger, R. W., Kalodimos, C. G., Kaptein, R., Vorgias, C. E., & Boelens, R. (2004). An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility. FEBS Letters, 563(1-3), 49-54. https://doi.org/10.1016/S0014-5793(04)00247-9