Table 2.

Displacements from closed βI domains

Conformation Cα root mean square deviation 
 β1-α1 loop α1 helix α1′ helix 
 Å Å Å 
Cocked β2 1.5 2.4 2.9 
Uncocked β2 1.2 0.9 0.6 
Intermediate β1 1.3 0.7 0.2 
Intermediate β3 1.9 1.5 1.5 
Intermediate state 6 β3 1.6 0.8 0.4 
Intermediate state 7 β3 1.6 3.5 1.3 
Final state 8 β3 2.1 4.4 3.8 
Open β3 2.1 4.3 4.0 
Conformation Cα root mean square deviation 
 β1-α1 loop α1 helix α1′ helix 
 Å Å Å 
Cocked β2 1.5 2.4 2.9 
Uncocked β2 1.2 0.9 0.6 
Intermediate β1 1.3 0.7 0.2 
Intermediate β3 1.9 1.5 1.5 
Intermediate state 6 β3 1.6 0.8 0.4 
Intermediate state 7 β3 1.6 3.5 1.3 
Final state 8 β3 2.1 4.4 3.8 
Open β3 2.1 4.3 4.0 

β1, β2, and β3 βI domains were superimposed on their closed counterparts. Differences in position were determined for β2 residues Y115–M117 (β1-α1 loop), D120–V124 (α1 helix), and G128–I138 (α1′ helix) and their equivalents in other β subunits. Structures use the following PDB ID numbers: intermediate β1 (3VI4) and its closed counterpart (3VI3); intermediate β3 (1L5G) and its closed counterpart (1JV2); β3 intermediate state 6 (3ZE2; chain B), state 7 (3ZDZ; chain B), final state 8 (3ZE2; chain D), and open β3 (2VDR) and their closed counterpart (3T3P).

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