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. 2015 Jul 24;4:e08811. doi: 10.7554/eLife.08811

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© 2015, Nithianantham et al

This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

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Figure 7. — (A) A refined 24 Å TBC-DEG-Q73L:αβ-tubulin:TBCC 3D map shown in three rotated views. The map shows conformational changes in tubulin density and the presence of new densities in the hollow core of the cage. (B) A segmented 24 Å TBC-DEG-Q73L:αβ-tubulin:TBCC map shown in three rotated views. The tubulin dimer density (red) is deformed by two new densities: a TBCC wedge shaped density engages the Arl2 interface (green), and a second density (cyan) is wedging between the two αβ-tubulin dimer lobes (red). (C) A TBC-DEG:αβ-tubulin:TBCC linear domain map shown to length scale. TBCD (pink, top panel) is composed of HEAT repeats. TBCE (second panel) includes a Cap-Gly domain (dark blue), a leucine rich repeat (LRR) domain (blue), and a ubiquitin-like domain (cyan). TBCC consists of a spectrin domain (yellow) and a C-terminal β-helix domain (green) (described in Figure 5), and Arl2 (third panel) consists of a GTPase fold (orange). αβ-tubulin (red) is shown in the bottom panel. Colors correspond to subunits shown in D–I. (D) A pseudo-atomic model of the TBC-DEG-Q73L:αβ-tubulin:TBCC ternary complex showing the interfaces of the TBCC β-helix catalytic domain (described in Figure 5, green) engaging Arl2 (orange) on top of TBCD (pink) while bound by the TBCE LRR bow (blue), while the α and β-tubulins are wedged by the ubiquitin domain (cyan). The α and β-tubulin coordinates were fit individually due to deformation in the tubulin intra-dimer interface in this map. The TBCC N-terminal spectrin domain (yellow) was fit into a density added to the floor segment. (E) A 90° vertically rotated view of that shown in D. (F) A 90° horizontally rotated view of that shown in D. (G) A central slice view of a 90° counterclockwise horizontally rotated view of that shown in D. The TBCC C-terminal catalytic domain engages Arl2 and binds the αβ-tubulin at the deformed intra-dimer interface with its unique loop (pink ribbon). Video 3 shows the C–F views. (H) Comparison of αβ-tubulin conformation based on αβ-tubulin coordinates fit into the αβ-tubulin density from the TBC-DEG-Q73L:αβ-tubulin map shown in the left panel (−TBCC) compared to the αβ-tubulin coordinates fit into the αβ-tubulin density in the TBC-DEG-Q73L:αβ-tubulin:TBCC map shown on the right (+TBCC), showing the conformational change at its intra-dimer interface that is associated with TBCC binding. (I) Cartoon view of TBC-DEG domain organization comparable to the view shown in E. (J) Cartoon view of TBC-DEG domain organization comparable to the view shown in F.

DOI: http://dx.doi.org/10.7554/eLife.08811.023

Figure 7—figure supplement 1. — (A) A refined 24 Å TBC-DEG-Q73L:αβ-tubulin:TBCC 3D map shown in three rotated views. The map shows conformational changes in tubulin density and the presence of new densities in the hollow core of the cage. (B) A segmented 24 Å TBC-DEG-Q73L:αβ-tubulin:TBCC map shown in three rotated views. The tubulin dimer density (red) is deformed by two new densities: a TBCC wedge shaped density engages the Arl2 interface (green), and a second density (cyan) is wedging between the two αβ-tubulin dimer lobes (red). (C) A TBC-DEG:αβ-tubulin:TBCC linear domain map shown to length scale. TBCD (pink, top panel) is composed of HEAT repeats. TBCE (second panel) includes a Cap-Gly domain (dark blue), a leucine rich repeat (LRR) domain (blue), and a ubiquitin-like domain (cyan). TBCC consists of a spectrin domain (yellow) and a C-terminal β-helix domain (green) (described in Figure 5), and Arl2 (third panel) consists of a GTPase fold (orange). αβ-tubulin (red) is shown in the bottom panel. Colors correspond to subunits shown in D–I. (D) A pseudo-atomic model of the TBC-DEG-Q73L:αβ-tubulin:TBCC ternary complex showing the interfaces of the TBCC β-helix catalytic domain (described in Figure 5, green) engaging Arl2 (orange) on top of TBCD (pink) while bound by the TBCE LRR bow (blue), while the α and β-tubulins are wedged by the ubiquitin domain (cyan). The α and β-tubulin coordinates were fit individually due to deformation in the tubulin intra-dimer interface in this map. The TBCC N-terminal spectrin domain (yellow) was fit into a density added to the floor segment. (E) A 90° vertically rotated view of that shown in D. (F) A 90° horizontally rotated view of that shown in D. (G) A central slice view of a 90° counterclockwise horizontally rotated view of that shown in D. The TBCC C-terminal catalytic domain engages Arl2 and binds the αβ-tubulin at the deformed intra-dimer interface with its unique loop (pink ribbon). Video 3 shows the C–F views. (H) Comparison of αβ-tubulin conformation based on αβ-tubulin coordinates fit into the αβ-tubulin density from the TBC-DEG-Q73L:αβ-tubulin map shown in the left panel (−TBCC) compared to the αβ-tubulin coordinates fit into the αβ-tubulin density in the TBC-DEG-Q73L:αβ-tubulin:TBCC map shown on the right (+TBCC), showing the conformational change at its intra-dimer interface that is associated with TBCC binding. (I) Cartoon view of TBC-DEG domain organization comparable to the view shown in E. (J) Cartoon view of TBC-DEG domain organization comparable to the view shown in F.

DOI: http://dx.doi.org/10.7554/eLife.08811.023