An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility
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Updated: Aug 25, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Michael A Durney1, Rainer W Wechselberger, Charalampos G Kalodimos
1Bijvoet Center for Biomolecular Research, Universiteit Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands.
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.
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