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. 2012 Mar 28;287(22):18510–18523. doi: 10.1074/jbc.M111.331199

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 2. — Domain 3 of subunit D of RNAP from M. acetivorans is predicted to bind two [4Fe-4S] clusters similar to two-[4Fe-4S] cluster ferredoxin. A, schematic of the domain architecture of M. acetivorans subunit D, including an amino acid alignment of domain 3 (MaRpoD (D3)) to two-[4Fe-4S] cluster ferredoxin (MA0431) from M. acetivorans. Conserved residues are indicated by an asterisk, including the cysteine residues postulated to bind the two [4Fe-4S] clusters. D1–D3, domains 1–3. B, homology model of the heterodimer of M. acetivorans subunit D (red) and subunit L (yellow) D-L heterodimer. The two [4Fe-4S] clusters in domain 3 are represented by sphere models. C, close-up view of domain 3 of subunit D showing putative cysteine ligands to each [4Fe-4S] cluster. The two [4Fe-4S] clusters in domain 3 are represented in stick models.