OhrR: Difference between revisions

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==Structure of Reduced OhrR ''Xc''==
==Structure of Reduced OhrR ''Xc''==
The resulting model 2pex shows the biologically relevant dimer of the protein. Each subunit of the dimer is composed of six α-helices and 3 β-strands.  
The resulting model 2pex shows the biologically relevant dimer of the protein. Each subunit of the dimer is composed of six α-helices and 3 β-strands.  
The specific residues corresponding to these regions of secondary structure are as follows.
The specific residues corresponding to these regions of secondary structure are as follows: α1 (residues 21–39), α2 (residues 47–58), β1(residues 62–63), α3 (residues 64–71), α4 (residues 75–87), β2 (residues 91–94), β3 (residues 104–107), α5 (residues 109–129), α6 (residues 133–151),  and three-ten helices 1a (residues 13–15) and 1b (residues 17–19).  
 
1. α1 (residues 21–39)
2. α2 (residues 47–58),
3. β1(residues 62–63),  
4. α3 (residues 64–71),  
5. α4 (residues 75–87),  
6. β2 (residues 91–94),  
7. β3 (residues 104–107),  
8. α5 (residues109–129),  
a. longest helix
b. displays a kink that is centered about residue G119.
9. α6 (residues 133–151)
 
10. two single-turn 310 helices N-terminal to helix α1:
a. 1a (residues 13–15)  
b. 1b (residues 17–19).  


The winged-HTH DNA-binding motif  
The winged-HTH DNA-binding motif  
- Formed by helices α3 and α4 followed by β strands β2 and β3, which form a small β sheet with β1.
- Formed by helices α3 and α4 followed by β strands β2 and β3, which form a small β sheet with β1.
-
 
α5 (residues109–129), longest helix
b. displays a kink that is centered about residue G119.


Interface
Interface
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