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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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.
|Digital Object Identifier (DOI):||doi:10.1016/S0014-5793(04)00247-9|
|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
|Accepted Date and Publication Date:||
|Date Deposited:||22 Feb 2006|
|Last Modified:||06 Aug 2015 02:19|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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