Crystal structure of yeast PriL-CTD at 1.55 Å.
(A) Ribbon diagram of the PriL-CTD. The larger N-terminal domain is coloured in red and the smaller C-terminal domain in blue. The Fe-S cluster cofactor is shown in space-fill representation; the Fe and S atoms are in red and yellow, respectively. (B) Topology diagram of the PriL-CTD; the numbering and residue span of each alpha helix is indicated. The cysteine residues that ligate the Fe-S cluster are explicitly indicated. Colouring as in panel (A). (C) Close-up view of the Fe-S cluster. Hydrophobic residues surrounding the Fe-S cluster are shown. The main-chain trace of the PriL-CTD is shown as a thin tube, whereas the Fe-S cluster and side chains are drawn as sticks.