Organization of protein domains in MinE and model of the cross-β structure formed by the amyloidogenic region of MinE. Ya-Ling Chiang Yuan-Chih Chang I-Chen Chiang Huey-Ming Mak Ing-Shouh Hwang Yu-Ling Shih 10.1371/journal.pone.0142506.g001 https://plos.figshare.com/articles/figure/_Organization_of_protein_domains_in_MinE_and_model_of_the_cross_946_structure_formed_by_the_amyloidogenic_region_of_MinE_/1601072 <p><b>(A)</b> The MinE protein can be divided into three functional domains, a membrane-binding domain that contains a membrane-induced amphipathic helix and basic residues, a bifunctional domain that interacts with MinD in an α-helical conformation and self-assembles in a β-stranded conformation, and a dimerization domain at the C-terminus. The dimerization domain is also known as the topological specificity domain. <b>(B)</b> Illustration of the cross-β structure formed by the amyloidogenic region of MinE (19–28); the alternating β strands are colored green and yellow for clarity. <b>(C)</b> RMSD plots of α-carbon and main-chain atoms from a 5-ns simulation to demonstrate conformational equilibrium. <b>(D)</b> Frontal view of the cross-β structure of the amyloidogenic region of MinE<sup>1-31</sup>; only the backbone of the molecule and the side chains facing the hydrophobic interface are shown. <b>(E)</b> Top view of the model showing anti-parallel arrangements of the residues in the amyloidogenic region; residues containing side chains facing the hydrophobic interface of two β sheets are shown in red.</p> 2015-11-12 02:50:19 Atomic Force Microscopy Characterization fibril morphology Lipid Bilayer Amyloid fibrils division protein MinE substrate surfaces amyloid formation Amyloidogenic Region fibril structures Bacterial Protein MinE protein fibrils time progression fibril structure protofibril organization force microscopy fibrillation processes nanotechnology applications