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![[Figure 2]](rr5201fig2mag.jpg)
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Figure 2
Crystals of TrpR. (a) Domain-swapped (top; PDB entry 1mi7; Lawson et al., 2004  ) and dimeric (bottom; PDB entry 1jhg; Lawson, 1996) structures of TrpR in a schematic ribbon view. The four polypeptide chains comprising one dimer-like `node' (black dashed oval) of the domain-swapped structure, as defined in the text, are shown with each in a different color. (b) Unit-cell contents and channels of ds-TrpR crystals. One unit cell is outlined in light blue, with the single polypeptide chain corresponding to the asymmetric unit represented in dark blue and the other polypeptide chains represented by gray ribbons. The orientations of the upper and lower assemblies correspond to those of the upper and lower schematics in (c). The continuous channel identified by MOLE analysis (MOLEonline 2.5; Sehnal et al., 2013; Pravda et al., 2018) as described in the text is represented by overlapping pale red spheres of radius 26.3–26.8 Å that fill two half-unit cells. (c) Schematic representation of the solvent channels in their presumed orientation with respect to the macroscopic shape of TrpR crystals. Left, side view (top) and top view (bottom) of the hexagonal bipyramidal crystals corresponding to the orientations in (b). Right, cartoons of the channels illustrating that they continue as linear pores through the crystal. |
![[Figure 2]](rr5201fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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