 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](jb5024fig1mag.jpg)
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Figure 1
Dimeric and domain-swapped TrpR structures. (a) Dimeric Val58Ile TrpR (PDB entry 1jhg; Lawson, 1996a  ) and (b) domain-swapped wild-type TrpR (PDB entry 1mi7; Lawson et al., 2004) in schematic ribbon view. The four polypeptide chains comprising one dimer-like `node' (black dashed oval) of the domain-swapped structure as described in the text are shown, each in a different color. L-Trp ligands in stick representation are enclosed in red ovals in the dimer; dashed red ovals mark equivalent positions in the domain-swapped structure, highlighting how each site in the domain-swapped node comprises residues arising from three chains, rather than from two as in the dimer. The N-termini of all chains are marked by black and gray filled circles, with black indicating a position in front of the plane of the page and gray a position behind the page. |
![[Figure 1]](jb5024fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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