Extended Data Fig. 5: The dimerization interface in the SPT–ORMDL3 complex. | Nature Structural & Molecular Biology

Extended Data Fig. 5: The dimerization interface in the SPT–ORMDL3 complex.

From: Structural insights into the assembly and substrate selectivity of human SPT–ORMDL3 complex

Extended Data Fig. 5: The dimerization interface in the SPT–ORMDL3 complex.

a, Structure of a dimer of SPTLC1SPTLC2 heterodimers. The dimer-dimer interface contains only limited interactions in the cytosol, which mainly involve the small helix α1 of SPTLC1 and the α6-β4 loop of SPTLC2. b, Biochemical validation of the structurally revealed dimer-dimer interface. The Mut2T variant of the SPT complex eluted around 1.5 ml later than the WT SPT complex in SEC. c, Representative cryo-EM micrograph and 2D class averages of the SPT Mut2T variant. d, The SPT Mut2T variant showed enzymatic activity comparable to that of the WT SPT complex when challenged with L-serine and palmitoyl-CoA. Uncropped image for b and data for graph d are available as source data.

Source data

Back to article page