Figure 2. Structural analysis of s-Mgm1.... | Rockefeller University Press

Figure 2.

$Figure 2. Structural analysis of s-Mgm1. (A) EM analysis of a negatively stained 2D crystal of s-Mgm1. The power spectrum calculated from the raw image is shown in the inset and shows strong diffraction up to 3 nm resolution. (B) P3 symmetrized projection map of s-Mgm1, calculated from merged data from nine processed images of negatively stained s-Mgm1 2D crystals. 2 × 2 unit cells are shown. One unit cell has dimensions of a = b = 200 Å, γ = 120°. (C) 3D reconstruction from images of tilted negatively stained 2D crystals of s- Mgm1 as seen from the direction perpendicular to the membrane plane. 2 × 2 unit cells are shown. (D) Homology model for s-Mgm1. This model was created using Modeller (Martí-Renom et al., 2000) and is based on the structures of dynamin A, dynamin-1, and a bacterial dynamin-like protein (PDB accession nos. 1JWY, 2AKA, and 2J69). The monomer is depicted as seen from the dimer interface. The model is color coded as follows: the GTPase domains is yellow, the GED is blue, and the pair of helices that putatively bind the membrane are orange. GDP–Mg complexes are depicted as spheres. (E) Schematic representation of the proposed parallel s-Mgm1 dimer bound to a lipid bilayer. The homology-modeled dimer and the corresponding 3D reconstruction based on the 2D crystallographic data are shown at the same scale. One monomer is colored as in D. Bars: (A) 200 nm; (C) 10 nm; (E) 5 nm.$

Structural analysis of s-Mgm1. (A) EM analysis of a negatively stained 2D crystal of s-Mgm1. The power spectrum calculated from the raw image is shown in the inset and shows strong diffraction up to 3 nm resolution. (B) P3 symmetrized projection map of s-Mgm1, calculated from merged data from nine processed images of negatively stained s-Mgm1 2D crystals. 2 × 2 unit cells are shown. One unit cell has dimensions of a = b = 200 Å, γ = 120°. (C) 3D reconstruction from images of tilted negatively stained 2D crystals of s- Mgm1 as seen from the direction perpendicular to the membrane plane. 2 × 2 unit cells are shown. (D) Homology model for s-Mgm1. This model was created using Modeller (Martí-Renom et al., 2000) and is based on the structures of dynamin A, dynamin-1, and a bacterial dynamin-like protein (PDB accession nos. 1JWY, 2AKA, and 2J69). The monomer is depicted as seen from the dimer interface. The model is color coded as follows: the GTPase domains is yellow, the GED is blue, and the pair of helices that putatively bind the membrane are orange. GDP–Mg complexes are depicted as spheres. (E) Schematic representation of the proposed parallel s-Mgm1 dimer bound to a lipid bilayer. The homology-modeled dimer and the corresponding 3D reconstruction based on the 2D crystallographic data are shown at the same scale. One monomer is colored as in D. Bars: (A) 200 nm; (C) 10 nm; (E) 5 nm.