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| | ==NMR structure of the N-terminal domain of trout cardiac troponin C at 7 C== | | ==NMR structure of the N-terminal domain of trout cardiac troponin C at 7 C== |
| - | <StructureSection load='1r6p' size='340' side='right'caption='[[1r6p]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''> | + | <StructureSection load='1r6p' size='340' side='right'caption='[[1r6p]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r6p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oncmy Oncmy]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R6P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r6p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R6P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r2u|1r2u]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6p OCA], [http://pdbe.org/1r6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r6p RCSB], [http://www.ebi.ac.uk/pdbsum/1r6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6p ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6p OCA], [https://pdbe.org/1r6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6p RCSB], [https://www.ebi.ac.uk/pdbsum/1r6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7ZZB9_ONCMY Q7ZZB9_ONCMY] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Troponin|Troponin]] | + | *[[Troponin 3D structures|Troponin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oncmy]] | + | [[Category: Oncorhynchus mykiss]] |
| - | [[Category: Blumenschein, T M]] | + | [[Category: Blumenschein TM]] |
| - | [[Category: Gillis, T E]] | + | [[Category: Gillis TE]] |
| - | [[Category: Sykes, B D]] | + | [[Category: Sykes BD]] |
| - | [[Category: Tibbits, G F]] | + | [[Category: Tibbits GF]] |
| - | [[Category: Ef-hand]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
Q7ZZB9_ONCMY
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Blumenschein TM, Gillis TE, Tibbits GF, Sykes BD. Effect of temperature on the structure of trout troponin C. Biochemistry. 2004 May 4;43(17):4955-63. PMID:15109253 doi:10.1021/bi035504z
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