Table 1 Correlation between the predicted effect of the mutations on TLDc domain stability and interaction between the mutants and V-ATPase.

From: The evolutionary conserved TLDc domain defines a new class of (H+)V-ATPase interacting proteins

Mutation: mouse Ncoa7/zebrafish Oxr2

ΔΔG, kcal/mol

Predicted relative effect of the mutation on TLDc domain stability

Interaction with V-ATPase (in pull-downs)

G802A/G660A

0.84

Small (< 1)

 +++ 

G815A/G673A

1.97

Medium (> 1, < 2)

−

S817A/S675A

0.71

Small (< 1)

 ++ 

G845A/G703A

1.44

Medium (> 1, < 2)

−

G896A/G754A

1.31

Medium (> 1, < 2)

−

L926A/L784A

2.42

Large (> 2)

 + 

E938A/E796A

0.74

Small (< 1)

 ++ 

  1. ΔΔG, the change in the change in Gibbs free energy between the folded and unfolded states (ΔG folding) and the change in ΔG folding when a point mutation is present, were calculated by PoPMuSiCv3.1. The smaller value of ΔΔG predicts smaller effect on TLDc domain stability. −, interaction undetectable; +++, interaction is similar to non-mutated (wild-type) protein; ++ and +, reduced and strongly reduced interaction.
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