10.1371/journal.pone.0142506.g001
Ya-Ling Chiang
Ya-Ling
Chiang
Yuan-Chih Chang
Yuan-Chih
Chang
I-Chen Chiang
I-Chen
Chiang
Huey-Ming Mak
Huey-Ming
Mak
Ing-Shouh Hwang
Ing-Shouh
Hwang
Yu-Ling Shih
Yu-Ling
Shih
Organization of protein domains in MinE and model of the cross-β structure formed by the amyloidogenic region of MinE.
Public Library of Science
2015
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
2015-11-12 02:50:19
Figure
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>