Skip to main content
. 2009 Jun 16;284(32):21707–21718. doi: 10.1074/jbc.M109.002709

FIGURE 3.

FIGURE 3.

Sequence alignment of T. thermophilus SoxB with other SoxB proteins and E. coli 5′-nucleotidase. The proteins analyzed are T. thermophilus HB27 SoxB (Tthe), Aquifex aeolicus VF5 SoxB (Aaeo), P. pantotrophus SoxB (Ppan), Chlorobium tepidum TLS SoxB (Ctep), and E. coli 5′-nucleotidase (5-NT). Numbering is that of the precursor proteins. However, only the mature amino acid sequences are shown. Residues that are invariant between the SoxB proteins in the alignment are shown in white on a black background. Residues that are similar between SoxB proteins in the alignment at a threshold of 75% using the BLOSUM62 substitution matrix (64) have a gray background. Secondary structure elements above the alignment are those of T. thermophilus SoxB, and those below the alignment are those of E. coli 5′-nucleotidase (Protein Data Bank entry 1HPU). Rectangles denote α-helices, and arrows show β-strands. The numbering of these elements follows that of the E. coli 5′-nucleotidase structure. *, ligands of metal site A. ●, ligands of metal site B. §, second sphere metal ligands in SoxB. ▼, residues directly or indirectly involved in substrate binding.