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![[Figure 1]](yt5033fig1mag.jpg)
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Figure 1
Crystal structure of the spiral hexamer structure of wt SV40 T-ag OBD shown as a ribbon diagram. (a) This `top' view is looking down the sixfold axis. A close-up view of the area bounded by the black box is shown in (c). (b) This `side' view is rotated ∼90° relative to the view in (a) and clearly shows the `gap'. Alternating monomers of T-ag OBD are colored cyan and green, respectively. The residues Phe151, Cys216 and Asp256 are shown as orange, yellow and magenta spheres, respectively. (c) A close-up view of the interface showing Phe151 (orange) and Asp256 (magenta) as sticks. Note that there are no side chains modelled for the Asp256 residue. (d) A molecular model of the disulfide bridge that could form between F151C and D256C. The S atoms are colored yellow. |
![[Figure 1]](yt5033fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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