 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](rr5056fig1_combined_mag.jpg)
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Figure 1
Stereoview of the N-terminal domain of LegC3. (a) Cartoon representation of the molecule. The four-helix bundle is at the top of the coiled-coil and extends through almost the entire range of the molecule. The molecule is coloured progressively from blue at the N-terminus to red at the C-terminus. The helical bundle is composed of two helices from the N-terminus and two from the C-terminus, and the coiled-coil constitutes an insertion between them. (b) Amino-acid sequence of LegC3. The expressed LegC3N contained residues 2–367. The light-shaded boxes show residues that are not observed in the crystal structure. The α-helices are boxed. The predicted transmembrane helices (TMs) are enclosed in dark-shaded boxes. The C-terminal domain starts at Ala425. (c) The leucines and isoleucines (shown in stick representation) contribute to the packing of helices within the coiled-coil. (d) Representative 2Fo – Fc electron density contoured at the 1σ level around a segment of the coiled-coil encompassing residues 95–106 and 180–191. Leucines are shown in yellow and isoleucines in wheat. |
![[Figure 1]](rr5056fig1_combined.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
