%0 Figure %A Chiang, Ya-Ling %A Chang, Yuan-Chih %A Chiang, I-Chen %A Mak, Huey-Ming %A Hwang, Ing-Shouh %A Shih, Yu-Ling %D 2015 %T Organization of protein domains in MinE and model of the cross-β structure formed by the amyloidogenic region of MinE. %U 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 %R 10.1371/journal.pone.0142506.g001 %2 https://plos.figshare.com/ndownloader/files/2437771 %K Atomic Force Microscopy Characterization %K fibril morphology %K Lipid Bilayer Amyloid fibrils %K division protein MinE %K substrate surfaces %K amyloid formation %K Amyloidogenic Region %K fibril structures %K Bacterial Protein MinE %K protein fibrils %K time progression %K fibril structure %K protofibril organization %K force microscopy %K fibrillation processes %K nanotechnology applications %X

(A) 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) 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. (C) RMSD plots of α-carbon and main-chain atoms from a 5-ns simulation to demonstrate conformational equilibrium. (D) Frontal view of the cross-β structure of the amyloidogenic region of MinE1-31; only the backbone of the molecule and the side chains facing the hydrophobic interface are shown. (E) 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.

%I PLOS ONE