1r6p
From Proteopedia
(New page: 200px<br /><applet load="1r6p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6p" /> '''NMR structure of the N-terminal domain of tr...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1r6p.jpg|left|200px]]<br /><applet load="1r6p" size=" | + | [[Image:1r6p.jpg|left|200px]]<br /><applet load="1r6p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r6p" /> | caption="1r6p" /> | ||
'''NMR structure of the N-terminal domain of trout cardiac troponin C at 7 C'''<br /> | '''NMR structure of the N-terminal domain of trout cardiac troponin C at 7 C'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Adaptation for life at different temperatures can cause changes in many | + | 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== | ==About this Structure== | ||
| - | 1R6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1R6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6P OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Oncorhynchus mykiss]] | [[Category: Oncorhynchus mykiss]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blumenschein, T | + | [[Category: Blumenschein, T M.]] |
| - | [[Category: Gillis, T | + | [[Category: Gillis, T E.]] |
| - | [[Category: Sykes, B | + | [[Category: Sykes, B D.]] |
| - | [[Category: Tibbits, G | + | [[Category: Tibbits, G F.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: ef-hand]] | [[Category: ef-hand]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:44 2008'' |
Revision as of 12:47, 21 February 2008
|
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 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 Thu Feb 21 14:47:44 2008
