Fig. 2: MIRO1-TRAK1 contact surfaces and dimerization.
From: Structural-functional characterization of the MIRO1-TRAK1 complex
a Structure of the MIRO11-591-TRAK1569-623 dimeric complex, with MIRO1 monomers shown in cyan and gray and Site-2 of TRAK1 in red. Red cylinders indicate the likely location of the transmembrane helices as they extend from the structure. b Contact surfaces (yellow) of Site-2 on MIRO1 (1915 Å2, top) and MIRO1 on Site-2 (2065 Å2, bottom). c MIRO1 dimerization interface shown as a surface representation (cyan, left) and a ribbon diagram (right). ELM2, ELM2-cGTPase linker, and cGTPase are colored orange, magenta, and blue, respectively. Contact surface areas were calculated using the SPPIDER server (https://sppider.cchmc.org/). d Anti-parallel β-sheet formed by TRAK1 residues Q575-V577. e The last observed MIRO1 residue in the structure, L587, is positioned <20 Å from its counterpart in the other dimer subunit, suggesting that the transmembrane helices are closely spaced as they insert into the outer mitochondrial membrane. f Representative mass photometry data for MIRO11-591 alone and with TRAK1569-623 from fraction 16 (see also Supplementary Fig. 5). Mass photometry and cryo-EM samples were prepared using GraFix36. Data are presented as histograms normalized to the bin with the highest number of counts (bin width = 6.1 kDa). The average mass, standard deviation, and percent of counts are derived from Gaussian fits.
