1. Volume 24, Issue 9, Pages 1488-1498 (September 2016)
Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol- Dependent Cytolysins 
Sara L. Lawrence, Michael A. Gorman, Susanne C. Feil, Terrence D. Mulhern, Michael J. Kuiper, Adam J. Ratner, Rodney K. Tweten, Craig J. Morton, Michael W. Parker 
Structure 
Volume 24, Issue 9, Pages (September 2016)
DOI: /j.str
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2. Structure 2016 24, 1488-1498DOI: (10.1016/j.str.2016.06.017)
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3. Figure 1 Crystal Structures of the CDC-CD59 Complexes
The structures are shown in ribbon representation. D1 is colored red, D2 cyan, D3 yellow, and D4 dark blue. The TMH1 and TMH2 regions are colored mauve. Two of the membrane-sensing loops of D4 (Trp-rich UDP loop and L1 loop housing the cholesterol-recognition motif) and the D4 β tongue are indicated. CD59D22A is gray.
(A) VLYml-CD59D22A.
(B) ILYml-CD59D22A.
(C) VLYml-CD59D22A.
(D) ILYml-CD59D22A.
See also Figures S1 and S3.
Structure  , DOI: ( /j.str )
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4. Figure 2 Detailed Views of the Interactions between CD59 and the CDCs
The proteins were oriented by superimposing the CD59D22A molecule of the VLYml-CD59D22A complex onto the CD59D22A of the ILYml-CD59D22A complex. Interfacial residues mentioned in the text are shown with key residues labeled, with those from CD59D22A in italics. The UDP loop is labeled with the Thr-Leu cholesterol-recognition motif (CRM) residues on L1 indicated.
(A–C) VLYml (blue) and CD59D22A (gray).
(D–F) ILYml (green) and CD59D22A (orange).
Close-up views are shown of the CD59D22A-CDC interfaces for VLYml (B and C) and ILYml (E and F) with the Y-X-Y-X14-R-S CD59-motif residues and their contact residues in CD59D22A labeled.
See also Figures S2, S5, and S6.
Structure  , DOI: ( /j.str )
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5. Figure 3 SAXS Analysis of the ILYml-CD59D22A Complex
Orthogonal views of the optimal superposition of the best fitting SAXS-derived ab initio shape envelope with the ILYml-CD59D22A crystal structure. The averaged filtered shape envelope from DAMAVER (Volkov and Svergun, 2003), derived from the best matching cluster of 8 DAMMIF models from a total of 30, is shown in cyan spheres and has been optimally superimposed on the ILYml-CD59D22A structure. ILYml is colored as in Figure 1 (domains colors of red, yellow, cyan, and dark blue) and CD59D22A in gray.
See also Figure S4.
Structure  , DOI: ( /j.str )
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6. Figure 4
Superimposition of D4 of Available CDC Structures Showing the UDP and L1 Loops with Key Residues, Arginine and Glutamic Acid, from the UDP Loop
(A) Superimposition of all available CDC structures. Non-CD59 dependent CDCs are shown in gray and ILY structures in green.
(B) Superposition of VLYml chain A (blue) with PFO.
(C) Superposition of VLYml chain B with ILY.
Structure  , DOI: ( /j.str )
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7. Figure 5 Models of ILYml and VLYml Linear Oligomers and Prepores
(A) ILYml-CD59D22A linear oligomer modeled on the PLY oligomer (Lawrence et al., 2015; Marshall et al., 2015). ILY is shown in green and CD59 in orange.
(B) VLYml (Chain B)-CD59D22A linear oligomer modeled on the PLY oligomer (Lawrence et al., 2015; Marshall et al., 2015). VLY is shown in blue and CD59 in gray.
(C) ILYml-CD59D22A prepore modeled on the published PLY prepore (Tilley et al., 2005). One protomer of the complex is highlighted with ILY is shown in green and CD59 in orange.
(D) VLYml-CD59D22A prepore modeled on the published PLY prepore (Tilley et al., 2005). One protomer of the complex is highlighted with VLY is shown in blue and CD59 in gray.
Structure  , DOI: ( /j.str )
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