Figure 1
The amino acid sequences of cytochrome b562 and 4TM.
The wall-eye stereo view of (A) the superimposed structures of cytochrome b562 (PDB: 3DE9, rainbow) and TM1-TM4 of cytochrome b from cytochrome bc1 complex (PDB: 3H1J, chain C, gray) and (B) the structure model of membrane-embedded 4TM showed in rainbow. The heme group in cytochrome b is presented as spheres and ball-and-stick in cytochrome b562. (C) The amino acid sequences of E. coli cytochrome b562 and 4TM are shown. The α-helixes of cytochrome b562 and the predicted TM helices of 4TM are delineated by bars. The underlines identify inserted sequences in 4TM used to elongate its TM segments. The residues highlighted in gray are identical in the corresponding sequence positions of both proteins. The position numbers indicate the starting positions of the reporter tags, BlaM and EGFP. (D) WB of the E. coli C41(ED3) membrane fraction after the expression of D94N-4TM-EGFP (right lane). The left lane shows the membrane fraction of E. coli that had been transformed with unmodified pET21-b(+). Protein was visualized by WB with an anti-His antibody against the His-tag of the fusion protein, where the His-tag is located between D94N fusion tag and 4TM.
