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Structure of the month

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Table 1.

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Figure 1.

Crystal structure of the activator. The two molecules of RACo in the asymmetric unit of the crystal are presented as cartoons. The left molecule (subunit A) contains all domains of the activator including the N-terminal domain (cyan), the linker domain (purple), the middle domain (blue) and the ASKHA domain (red). The second monomer (subunit B) is colored in grey and does not include the N-terminal domain in its structure. Magnesium and phosphate ions are indicated as green and gray spheres, respectively. The [2Fe-2S] cluster is shown as spheres colored red for iron and yellow for sulfur.

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Figure 2. 

Cartoon-representation of the ASKHA domain. The ASKHA domain of RACo (residues 207 – 630) is shown in (a). The conserved βββαβαβα topology of the ASKHA family is illustrated with β–strands in magenta and α–helices in marine. Surface representation of the four lobes of the ASKHA domain (IA, IB, IIA and IIB) in analogy to the ASKHA family proteins is given in (b).