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. 2022 Jun 17;13:3491. doi: 10.1038/s41467-022-31240-4

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a Cryo-EM map of an amyloid fibril from recombinant, full-length apo human SOD1 with the atomic model overlaid. The SOD1 fibril core comprises the N-terminal segment (residues 3–55) and the C-terminal segment (residues 86 to 153) colored green and purple, respectively, with an internal disordered segment. b Schematic view of the SOD1 fibril core. Residues are colored as follows: white, hydrophobic; green, polar; red and blue, negatively and positively charged, respectively; and magenta, glycine. β strands are indicated with bold lines. Side chains of most hydrophobic residues are located in the interior of the SOD1 fibril fold. c Sequence of the fibril core comprising residues 3–55 and 86–153 from full-length human SOD1 (1 to 153) with the observed six β strands colored violet (β1), blue (β2), light blue (β3), cyan (β4), light cyan (β5), and green (β6) in the N-terminal region and the observed seven β strands colored light green (β7), yellow (β8), gold (β9), orange (β10), pink (β11), magenta (β12), and light magenta (β13) in the C-terminal region. The dotted lines correspond to residues 1–2 and residues 56–85 not modeled in the cryo-EM density. d Ribbon representation of the structure of an SOD1 fibril core containing five molecular layers and two segments. e As in d, but viewed perpendicular to the helical axis, revealing that the height of one layer along the helical axis is 15.82 Å. f Electrostatic surface representation of the structure of an SOD1 fibril core containing five molecular layers and two segments. g Hydrophobic surface representation of the structure of an SOD1 fibril core as in d. f, g Three pairs of amino acids (Lys36 and Asp109; His43 and Asp101; and His46 and Glu100) form three salt bridges at the intramolecular interface between the N- and C-terminal regions of SOD1 fibril. The surface of two regions of the SOD1 fibril core is shown according to the electrostatic properties (red, negatively charged; blue, positively charged) (f) or the hydrophobicity (yellow, hydrophobic; blue, hydrophilic) (g) of the residues.