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


Durney, Michael A., Wechselberger, Rainer W., Kalodimos, Charalampos G., Kaptein, Robert, Vorgias, Constantinos E. and Boelens, Rolf (2004) An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility. Febs Letters, 563, (1-3), 49-54. (doi: 10.1016/S0014-5793(04)00247-9).

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Description/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.

Item Type: Article
ISSNs: 0014-5793 (print)
Related URLs:
Keywords: conformational flexibility, protein dynamics, thermostability, nuclear magnetic resonance spin relaxationdna-binding protein, histone-like protein, bacillus-stearothermophilus, thermostability, spectroscopy, c-13, ihf, purification, resonance
Subjects: Q Science > QD Chemistry
Q Science > QR Microbiology
Divisions: University Structure - Pre August 2011 > School of Chemistry
ePrint ID: 20187
Date Deposited: 22 Feb 2006
Last Modified: 27 Mar 2014 18:09
URI: http://eprints.soton.ac.uk/id/eprint/20187

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