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![[Figure 6]](dw5200fig6mag.jpg)
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Figure 6
The structures of (a) BcGDHγα, (b) W. succinogenes membrane-bound fumarate reductase (PDB entry 2bs2; Madej et al., 2006  ) and the flavoprotein shown in light green in (b) were superimposed onto the structure of BcGDHγα in (c). The colors of BcGDHγα are the same as in Fig. 2. The 3Fe–4S cluster is indicated by a red dotted circle. Soluble S. putrefaciens fumarate reductase was first superimposed onto the structure of the α-subunit of BcGDHγα with 3.0 r.m.s.d., and the membrane-bound fumarate reductase from W. succinogenes was superimposed onto the structure of soluble fumarate reductase from S. putrefaciens (with 1.8 r.m.s.d.). Consequently, the structure of the membrane-bound fumarate reductase was directly compared with the structure of BcGDHγα by removing the structure of the soluble fumarate reductase. (b) The two-molecule form of fumarate reductase is shown in the crystal structure (Lancaster et al., 1999). A molecule of fumarate reductase is represented in light pink (right). In the other molecule, subunit A (flavoprotein containing FAD covalently bound to His43), subunit B (iron–sulfur protein including 2Fe–2S, 4Fe–4S and 3Fe–4S clusters) and subunit C (transmembrane-spanning protein including diheme cytochrome b molecules) are colored light green, light orange and dark green, respectively. The bound FAD molecules in the structures are shown as orange stick models. The bound FAD and heme b molecules are shown as orange lines and magenta stick models, respectively. The iron–sulfur clusters are shown as sphere models. The other molecule of fumarate reductase colored light pink was deleted in (c) to clarify the positions of FAD, iron–sulfur clusters and heme b molecules, which are related to electron transfer. bP is the proximal heme and bD is the distal heme. |
![[Figure 6]](dw5200fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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