Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 Sep 6;7:10744. doi: 10.1038/s41598-017-11008-3

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2017

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/.

PMC Copyright notice

3D structure of Drp1 associated with a phosphatidylserine (PS) lipid template. (a) The primary sequence and tertiary structure (PDB ID: 4BEJ) of Drp1 highlights conserved domains: G domain (green), middle domain (blue), variable domain (orange) and GTPase effector domain (GED, blue). (b–c) Negative stain (b) and cryo-EM (c) images of Drp1 oligomerized in the presence of GMPPCP on galactosyl ceramide (GC) nanotubes containing phosphatidylserine (PS) at low (left; scale bar, 100 nm) and high magnifications (right; scale bar, 50 nm). Filled arrows indicate Drp1 decorated tubes, while open arrowheads indicate undecorated GC/PS tubes. (d–e) The 3D reconstruction of Drp1 on a GC/PS nanotube is presented. The helical pitch (13 nm) and diameter (51.4 nm) are indicated. (f) Cross-section of the 3D structure demonstrates the T-shaped architecture, and a gap between the protein and lipid is highlighted (open arrowhead). (g) The fitted structures of Drp1 GTPase (green) and stalk (blue) dimers are shown. The 80 loop interface (red) mediating G-domain dimerization is highlighted. (h) A side view of multiple Drp1 dimers fitted into the helical density. Unoccupied density is highlighted (dotted orange hexagon). (i) An end-on view of the same fitted structures.