Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis: Supplemental Video 2
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A supplemental video from the 2020 review by Roland Lill and Sven-A. Freibert, "Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis," from the Annual Review of Biochemistry: annualreviews.org/doi/10.1146/annurev-biochem-013118-
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Shown: Hypothetical movement of the conserved Cys-loop of NFS1. Morphing was done by UCSF Chimera (7) based on several loop intermediates in NFS1 or related bacterial SufS structures (loop “inside” and “outside”; Boniecki, Freibert et al., unpublished; (8, 9)). Color code is as in Supplemental video 1. The conserved Cys381 residue of human NFS1 receives a persulfide in its “inside” position when Cys381 is located close to the pyridoxal phosphate (PLP) moiety (shown as spheres) of NFS1. Subsequently, the Cysloop undergoes large conformational rearrangements, and Cys381 contacts ISCU2 at the NFS1 surface for persulfide transfer to ISCU2.
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