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Figure 1
Overall structure of HpGluRS. (a) The HpGluRS monomer in rainbow colors from blue at the N-terminus to red at the C-terminus. The glutamate-binding site is indicated in blue parentheses, while the tRNA-binding site is indicated in red parentheses. (b) Ribbon diagram calculated by ENDScript. The circumference of the ribbon (sausage) represents relative structural conservation compared with other GluRS structures (these structures are indicated in Supplementary Fig. S1). Thinner ribbons represent more highly conserved regions. In comparison, thicker ribbons represent less conserved regions, and the ribbon is colored by sequence conservation, with red indicating identical residues. (c) The solvent-accessible surface area of HpGluRS is colored by sequence conservation, with red indicating identical residues. (d) Superposed HpGluRS (gray) with Thermotoga maritima GluRS (TmGluRS; PDB entry 3afh, cyan; Ito et al., 2010BB12) reveals a conserved prototypical GluRS topology; a glutamyl-AMP analog (magenta sticks) is sitting in the glutamate-binding site. An ethylene glycol molecule from the cryoprotectant is shown as yellow sticks. (a)–(d) are shown in the same orientation.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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