Fig. 4 | Nature Communications

Fig. 4

From: Structural basis for functional interactions in dimers of SLC26 transporters

Fig. 4

Oxidative cysteine cross-linking between TM14 of SLC26Dg. a In gel GFP fluorescence analysis of disrupted E. coli cells expressing single-cysteine variants of SLC26Dg fused to superfolder GFP. Following oxidative cross-linking, samples were analyzed by non-reducing SDS-PAGE. Cysteine-free SLC26Dg (cysless) and L144C (TM5) represent negative controls. Black and white arrows indicate dimeric and monomeric SLC26Dg. Source data are provided as a Source Data file. b Side view of the SLC26Dg dimer model. Core and gate domain are colored orange and gray, respectively. Positions in TM14 susceptible to cross-linking are colored in green, non-susceptible residues are colored pink. The gate domain of the right protomer is depicted in surface representation. TM13 of the left protomer is contoured. The circled numbers indicate the respective TMs

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