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PDBsum entry 1r6p

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protein metals links
Metal binding protein PDB id
1r6p
Jmol
Contents
Protein chain
89 a.a. *
Metals
_CA
* Residue conservation analysis
PDB id:
1r6p
Name: Metal binding protein
Title: Nmr structure of the n-terminal domain of trout cardiac troponin c at 7 c
Structure: Troponin c. Chain: a. Fragment: n-terminal domain (residues 1-89). Engineered: yes
Source: Oncorhynchus mykiss. Rainbow trout. Organism_taxid: 8022. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
NMR struc: 40 models
Authors: T.M.Blumenschein,T.E.Gillis,G.F.Tibbits,B.D.Sykes
Key ref:
T.M.Blumenschein et al. (2004). Effect of temperature on the structure of trout troponin C. Biochemistry, 43, 4955-4963. PubMed id: 15109253 DOI: 10.1021/bi035504z
Date:
15-Oct-03     Release date:   08-Jun-04    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q7ZZB9  (Q7ZZB9_ONCMY) -  Troponin C
Seq:
Struc:
161 a.a.
89 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium ion binding     1 term  

 

 
DOI no: 10.1021/bi035504z Biochemistry 43:4955-4963 (2004)
PubMed id: 15109253  
 
 
Effect of temperature on the structure of trout troponin C.
T.M.Blumenschein, T.E.Gillis, G.F.Tibbits, B.D.Sykes.
 
  ABSTRACT  
 
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.