Structural variability within the Type 1 polymorphs.
A) Seven pairwise overlays of the wild-type 1A structure (PDB:6A6B) with other wild-type and mutant structures depicting the range of structural variability that is found in the Type 1 fold. The structural alignments were done by an LSQ-superposition of the Cα atoms of residues 51-66. The other Type 1 structures from left to right, top to bottom are wild-type 1A without buffer (PDB:6CU7), N-terminally acetylated wild-type 1A residues 1-103 (PDB:6OSM), the H50Q mutant 1M without buffer (PDB:6PEO), wild-type 1A in Tris buffered saline (PDB:7V4D), the patient-derived JOS 1M polymorph (PDB:8BQV), mix of wild-type and seven residue JOS-associated insertion mutant 1A in PBS (PDB:8CEB) and N-terminally acetylated wild-type 1M seeded from PD patient CSF in PIPES with 500 mM NaCl. B) Same overlay shown at the top right in A, showing the triad of lysine residues often formed at the interface in the presence of phosphate (PDB:6CU7) compared the inward facing orientation of K58 in the absence of phosphate (PDB:6A6B). The location of often observed density, thought to be PO42- is indicated with the pink sphere.