Figure 1.

LpoA^N Has a TPR Domain-like Structure

(A) Amino acid sequence of the LpoA^N construct used for structure determination and secondary structure elements (α helices). The residues of the oligohistidine tag are shown in red.

(B) Cartoon representation of the 20 lowest-energy structures of LpoA^N, as determined by NMR spectroscopy, emphasizing the spatial arrangement of the 12 α-helices, which are numbered from the N to C terminus.

(C) LpoA^N is stabilized by numerous interhelical hydrophobic contacts. The ten α helices with more than four residues are shown as circles and labeled according to the description in (B). Interhelical hydrophobic contacts are represented with dashed lines, and short plain lines connect each of the residues to its corresponding helix.

See also Figure S1.