1. Structure of TOR and Its Complex with KOG1
Alessandra Adami, Begoña García-Álvarez, Ernesto Arias-Palomo, David Barford, Oscar Llorca 
Molecular Cell 
Volume 27, Issue 3, Pages (August 2007)
DOI: /j.molcel
Copyright © 2007 Elsevier Inc. Terms and Conditions

2. Figure 1
Purification and Electron Microscopy of TOR1 and the TOR-KOG1 Complex
(A and B) Schematic representation of the domain organization of TOR (A) and KOG1 (B). Color codes are maintained throughout.
(C) SDS gels of the fractions collected for the purification of TOR1 (a) and the TOR-KOG1 complex (b). These fractions were pooled and concentrated (c, only TOR-KOG1 shown).
(D) Negatively stained electron microscopy field of TOR1 with some single molecules highlighted.
(E and F) Projections and averages at the last step of angular refinement for TOR1 (E) and TOR-KOG1 (F).
(G) Cryo-EM field of purified TOR-KOG1 complex, with some particles highlighted.
(H) Reference-free 2D averages of the particles extracted from the cryo-EM fields.
Molecular Cell  , DOI: ( /j.molcel )
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3. Figure 2 3D Structure of TOR1
(A) Back view of the EM structure of DNA-PKcs filtered at 25 Å resolution (Rivera-Calzada et al., 2005).
(B–E) Several views of the 3D structure of TOR1 to illustrate different regions of the map denoted by orange (N-terminal repeats), pink (PI3K domain), blue (FATC), green (FAT), and yellow (other). In (D), the putative position of the FRB domain is labeled with an asterisk.
Molecular Cell  , DOI: ( /j.molcel )
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4. Figure 3 3D Structure of TOR-KOG1
(A) Views of the EM structure of the TOR-KOG1 complex. Color code is as that in Figure 2, but EM density corresponding to KOG1 in the complex is shown as light blue. The putative location of the FRB domain is labeled with an asterisk.
(B) Approximate 3D map of KOG1 extracted from the TOR-KOG1 complex after subtracting TOR1 (a). The atomic structure of a WD40 protein (PDB file 2G9A) was fitted by using ADP_EM (Garzon et al., 2007) (b).
(C) Nanogold labeling of the C terminus of KOG1 tagged with a His10 in the TOR-KOG1 complex. Reference projections of the reconstruction were used to classify and average the data. The location of the gold is shown as a red dot on the 3D model.
(D) The KOG1 model is shown superimposed to the 3D structure of TOR1, depicting its approximate disposition within the TOR-KOG1 complex.
Molecular Cell  , DOI: ( /j.molcel )
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5. Figure 4 KOG1 and LST8 Recognize Specific Regions of TOR1
(A) Fragments constructed for segments spanning TOR1 and used for IVT are labeled 1–4.
(B) Radioactively labeled fragments of TOR were captured with tagged KOG1 and analyzed by SDS gel to detect binding to KOG1. (a) Specific fragments of TOR1 binding to KOG1. (b) Nonspecific binding to the beads. (c) Control reactions to verify the correct translation of KOG1 and the TOR1 fragments.
(C) As in (B) but pull-downs were performed with tagged LST8.
(D) Model proposed for the organization of the TOR-KOG1 complex and the recruitment of substrates.
Molecular Cell  , DOI: ( /j.molcel )
Copyright © 2007 Elsevier Inc. Terms and Conditions