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Protein Science, Vol 3, Issue 11 1961-1974, Copyright © 1994 by Cold Spring Harbor Laboratory Press
ARTICLE |
S. M. GAGNE, S. TSUDA, M. X. LI, M. CHANDRA, L. B. SMILLIE and B. D. SYKES
Department of Biochemistry, Medical Research Council Group in Protein Structure and Function, University of Alberta, Edmonton T6G 2H7, Canada
The backbone resonance assignments have been completed for the apo ((1)H and (15)N) and calcium-loaded ((1)H, (15)N, and (13)C) regulatory N-domain of chicken skeletal troponin-C (1-90), using multidimensional homonuclear and heteronuclear NMR spectroscopy. The chemical-shift information, along with detailed NOE analysis and (3)J(HNH{alpha}) coupling constants, permitted the determination and quantification of the Ca(2+)-induced secondary structural change in the N-domain of TnC. For both structures, 5 helices and 2 short {beta}-strands were found, as was observed in the apo N-domain of the crystal structure of whole TnC (Herzberg O, James MNG, 1988, J Mol Biol 203:761-779). The NMR solution structure of the apo form is indistinguishable from the crystal structure, whereas some structural differences are evident when comparing the 2Ca(2+) state solution structure with the apo one. The major conformational change observed is the straightening of helix-B upon Ca(2+) binding. The possible importance and role of this conformational change is explored. Previous CD studies on the regulatory domain of TnC showed a significant Ca(2+)-induced increase in negative ellipticity, suggesting a significant increase in helical content upon Ca(2+) binding. The present study shows that there is virtually no change in {alpha}-helical content associated with the transition from apo to the 2Ca(2+) state of the N-domain of TnC. Therefore, the Ca(2+)-induced increase in ellipticity observed by CD does not relate to a change in helical content, but more likely to changes in spatial orientation of helices.
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