Extended Data Fig. 5: Domain characterization of PDIA6.
From: A multichaperone condensate enhances protein folding in the endoplasmic reticulum
a, SEC elution profiles (solid lines, left axis) and MALS apparent molecular mass (dotted lines, right axis) of PDIA6 full-length (FL) and domains. b, Sequence alignment of helix α4 of PDI catalytically active domains. The extended helix α4 of PDIA6 is highlighted by a pink square. Residues forming the leucine-valine adhesive dimerization motif23 are marked by an orange square. Domain delimitations as defined on uniport.org or by available crystal structures. c, Structural comparison of PDI catalytically active domains helix α4. d, Mass photometry of PDIA6 at 50 nM and 25 nM. Occupancy and oligomeric state are indicated for each peak. e, Crystal structure of PDIA6 domain b at a resolution of 1.8 Å. f, Zoom on the electron density map of PDIA6 domain b crystal structure. g, Potential of mean force along the collective variable (CV). The free energy profile for the WT protein (274PPP276) has one minimum at ΔCV 0 (black), while the 274GGG276 linker is flexible in the 0–2 Å range and the free energy increases slower with CV distance (yellow). h, Protein logo analysis of PDIA6 of domain a-b linker of Homo sapiens, Rattus norvegicus, Mus musculus, Pongo abelii, Drosophila melanogaster and Caenorhabditis elegans. i, Thermal stability of reduced domain a (light grey), domain b (dark grey) and domain ab (pink)as determined by differential scanning fluorimetry.
