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![[Figure 6]](jb5033fig6mag.jpg)
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Figure 6
Comparison of the helical filament structure of the DREP3 CIDE domain with those of other CIDE domains. (a) Structural alignment of one turn comprised of nine molecules of the DREP3 CIDE domain with one turn comprised of eight molecules of the DREP2 CIDE domain (grey) revealing a conserved helical arrangement. A molecule of the DREP3 CIDE domain adjacent to the aligned molecule needs to rotate 18° to allow superimposition with the corresponding DREP2 CIDE domain. (b) Structural alignment of one turn comprised of nine molecules of the DREP3 CIDE domain with one turn comprised of ten molecules of the DREP4 CIDE domain (blue). A molecule of the DREP3 CIDE domain adjacent to the aligned molecule needs to rotate 20° to allow superimposition with the corresponding DREP2 CIDE domain. (c) A 360° surface view of the helical filament structure of the DREP3 CIDE domain with displayed electrostatics. The diameter of the hole formed in the helical filament is shown. (d, e) Electrostatic surface representations of the helical filament structures of the DREP2 (d) and DREP4 (e) CIDE domains. The diameters of the hole are provided. |
![[Figure 6]](jb5033fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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