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![[Figure 3]](dw5200fig3mag.jpg)
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Figure 3
Cysteine cluster of BcGDHγα. A unique cysteine cluster is formed by one cysteine from the γ-subunit and four cysteines from the α-subunit. Cys152 and Cys213 form a disulfide bond between the γ- and α-subunits. Cys212, Cys218 and Cys222 are involved in the iron–sulfur cluster (3Fe–4S). The identified positions of the 3Fe–4S cluster and the disulfide bond between the γ- and α-subunits are shown. Simulated-annealing OMIT maps of F3S (the 3Fe–4S iron–sulfur cluster) and five cysteine residues (Cys152, Cys212, Cys213, Cys218 and Cys222) in wild-type BcGDHγα contoured at 5σ are shown in light blue in (a)–(d). The 2Fo − Fc electron-density maps using the merged data sets of wild-type BcGDHγα collected at wavelengths of 1.0 and 1.74086 Å (after the initial refinement and before including F3S in refinement) are shown in blue and contoured at 5σ in (b), (c) and (d). S and Fe atoms are shown in yellow and orange, respectively. The identified 3Fe–4S cluster consists of three Fe atoms and four S atoms represented as spheres. |
![[Figure 3]](dw5200fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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