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. Author manuscript; available in PMC: 2016 Jan 14.
Published in final edited form as: FEBS Lett. 2011 Dec 9;586(1):60–63. doi: 10.1016/j.febslet.2011.11.024

Figure 3. Residues critical for SepCysS activity identified using in vivo screening.

Figure 3

The crystal structure of AfSepCysS (PDB: 2E7J) reveals that PLP is covalently linked to Lys209, and three residues coordinates a sulfate ion at the active site [8]. Our functional assay showed that Arg79, His103 and Tyr104 are all important for SepCysS activity, suggesting that these residues may interact with the phosphate group of Sep-tRNA, which is mimicked by the sulfate ion in the crystal structure. The region containing two critical residues Cys39 and Cys42 is disordered in the structure.