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![[Figure 2]](ud5051fig2mag.jpg)
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Figure 2
The 121 binding events on the surface of the TFE tetramer. The same view and coloring scheme are used as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif){kind=small} . The two α-subunits are colored wheat and green and the β2 thiolase dimer subunits are colored cyan and yellow. The ECH, HAD and KAT active sites are identified as ECH(CoA) (with a thin arrow), HAD(NAD+) and KAT(CoA). The vertical arrow visualizes the twofold axis of the α2β2 tetramer. The ECH active site of the left α-subunit (wheat) is behind and the ECH active site of the right α-subunit (green) is at the front, showing the fragments bound in its substrate-binding tunnel. The surface has been made transparent, so that binding events that are hidden behind the surface are still visible. The labels CoA-A, CoA-B and CoA-C identify the additional CoA binding sites. |
![[Figure 2]](ud5051fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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