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. 2007 Feb 14;104(8):2620–2625. doi: 10.1073/pnas.0611504104

Fig. 1.

Fig. 1.

The structure of M. maripaludis SepRS. (A) The synthetase is a tetramer with pseudo 222 symmetry and is shown in surface representation, and the color of each monomer differs. The surface of one of the monomers is transparent, revealing a ribbon representation of its structure. (B) The catalytic domains of the SepRS tetramer shown in the same orientation as in A. Superimposed on this core are the two α and two β chains of the T. thermophilus PheRS (18). (C) A monomer of SepRS in the same orientation, colored by domain and motif. (D) Representative electron density for a helix in motif 1. To provide an unbiased view, the map was calculated by using phases derived without the use of the model; phases were produced by solvent-flattening and NCS-averaging heavy atom-derived phases. The amplitudes were sharpened by a B factor of 100 and the contour level set at 2σ to reveal side-chain density. (E) A structure-based sequence alignment of the catalytic domains of M. maripaludis SepRS, M. jannaschii SepRS, and the α and β-chains of the T. thermophilus PheRS. The secondary structure elements of the M. maripaludis SepRS are indicated and colored as in C.