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![[Figure 1]](ud5051fig1mag.jpg)
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Figure 1
The TFE tetramer with its ECH, HAD and KAT active sites. Top: the two α-chains (wheat and green) are assembled on top of the β2 thiolase dimer (cyan, yellow). The vertical arrow visualizes the twofold axis of the α2β2 tetramer. The ECH, HAD and KAT active sites are labeled ECH(CoA) (with a thin arrow), HAD(NAD+) and KAT(CoA). CoAs bound at the additional CoA binding sites are labeled CoA-A, CoA-B and CoA-C. The curved thick arrows identify the path between the ECH and HAD active sites and between the HAD and KAT active sites. Bottom: schematic representation of the reactions catalyzed by the ECH, HAD and KAT active sites. |
![[Figure 1]](ud5051fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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