 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](jb5024fig3mag.jpg)
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Figure 3
Structures of Val58Ile ds-TrpR without and with L-Trp. The polypeptide chain is represented as a ribbon cartoon in orange for the structure without L-Trp and in green for the structure with L-Trp. (a) Overlay of one polypeptide chain from each structure, with the N- and C-termini labeled. The location of the mutation giving rise to the Val58Ile variant is indicated by a dashed oval, with an enlargement above showing the Val58 and Ile58 side chains as sticks in an overlay of the local structures of wild-type ds-TrpR with Val58 (blue; PDB entry 1mi7; Lawson et al., 2004  ) and of Val58Ile ds-TrpR with Ile58 (orange; this work). The L-Trp-binding region and its local surroundings including a water molecule (red oxygen sphere) are indicated by the dashed circle, where L-Trp is shown as sticks and the nearby residues Thr81, Arg84 and Ser88 (left to right) are shown as lines with atomic colors (oxygen, red; nitrogen, blue; carbon, same color as main chain). (b) The circled area in (a) is represented by a 2Fo − Fc electron-density map at contour level 1.0σ shown as a gray mesh surrounding Arg84 and the modeled ligands iPrOH (orange C atoms) and water (red oxygen sphere), with potential hydrogen-bond interactions with neighboring residues shown as dashed yellow lines. Only residues inferred to interact with the ligands are labeled. (c) As in (b) for the L-Trp-soaked structure. (d) Details of L-Trp binding, using the chain colors in (a), are shown for the structure of dimeric Val58Ile TrpR (PDB entry 1jhg; Lawson, 1996a). (e) As in (d) for the structure of Val58Ile ds-TrpR (this work). |
![[Figure 3]](jb5024fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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