1r6p
From Proteopedia
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NMR structure of the N-terminal domain of trout cardiac troponin C at 7 C
Overview
Adaptation for life at different temperatures can cause changes in many, aspects of an organism. One example is the expression of different protein, isoforms in species adapted to different temperatures. The calcium, regulatory protein cardiac troponin C (cTnC), from rainbow trout, (Oncorhynchus mykiss), is a good model for studying temperature effects, both because of its low physiological temperature and because mammalian, cTnC, extensively studied at higher temperatures, can be used for, comparison. We determined the structure and studied the backbone dynamics, of the regulatory domain of trout cardiac troponin C (ScNTnC) with one, Ca(2+) bound at 7 and 30 degrees C, using nuclear magnetic resonance, spectroscopy (NMR). The overall fold of the regulatory domain of trout, cTnC at both temperatures is similar to the regulatory domain of mammalian, (human, bovine, and porcine isoform) cTnC bound to one Ca(2+). By, comparing the trout structures at the two temperatures, we identify, differences between the positions of the helices flanking the calcium, binding loops, and the overall structure at 7 degrees C is more compact, than that at 30 degrees C. The structure at 7 degrees C is more similar to, the mammalian cTnC, which was determined at 30 degrees C, indicating that, they have the same conformation at their respective physiological, temperatures. The dynamic properties of the regulatory domain of trout, cTnC are similar at the two temperatures that were used in these studies.
About this Structure
1R6P is a Single protein structure of sequence from Oncorhynchus mykiss with CA as ligand. Full crystallographic information is available from OCA.
Reference
Effect of temperature on the structure of trout troponin C., Blumenschein TM, Gillis TE, Tibbits GF, Sykes BD, Biochemistry. 2004 May 4;43(17):4955-63. PMID:15109253
Page seeded by OCA on Sat Nov 24 22:14:58 2007
