 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](wd5146fig1mag.jpg)
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Figure 1
Crystal structure of TmTrpRS. (a) Schematic representation of the TmTrpRS crystallographic dimer. The α-helices are represented as cylinders in gray, β-strands as arrows in purple and the loops in pink in one monomer (top) of the dimer. The crystallographically related molecule below is color-coded from blue at the N-terminus to red at the C-terminus. The bound 4Fe–4S cluster and L-tryptophan are represented as sticks. The β-strands (β1–β5) and α-helices (α1–α15) are labeled (310-helices are not labeled). The ATP-binding motifs (HIGH and KMSKS) are highlighted in red. The short hinge region (residues 182–186) connecting the Rossmann-fold and the TAB domains is indicated. (b) Close-up view of a 2Fo − Fc OMIT map contoured at 1σ showing the iron–sulfur cluster bound to the cysteine motif [Cys236-x22-Cys259-x6-Cys266-x2-Cys269] in the anticodon-binding region (top box) and the L-tryptophan found in the active site (bottom box). (c) Comparison of TmTrpRS to the `open' and `closed' conformations of BsTrpRS. |
![[Figure 1]](wd5146fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
