Structural comparison of DndA with related cysteine desulfurases/selenocysteine lyase.

Abstract

<p>(<b>A</b>) Structural superimposition of DndA (red), IscS (green, PDB code 1P3W), NifS (cyan, PDB code 1ECX), CsdB (magenta, PDB code 1C0N), and SufS (blue, PDB code 1T3I). Their bound PLP's are shown as sticks. (<b>B</b>) In DndA, the active site Cys327 is located on a β strand, and its distance from PLP is ∼16 Å. In IscS (<b>C</b>) and NifS (<b>D</b>), the active site cysteines are located on relatively long loops, and are not visible in the crystal structure. Visible residues closest to the catalytic cysteines on the primary sequence are no less than 9 Å from PLP. In CsdB (<b>E</b>) and SufS (<b>F</b>), the active site cysteines are located on relatively short loops, and are ∼7 Å from PLP.</p