Annual Reviews Extra | Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis: Supplemental Video 3 @annualreviewsextra | Uploaded January 2020 | Updated October 2024, 2 hours ago.
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-
111540?utm_source=youtube&utm_medium=bi.lill&utm_campaign=suppvideo
Shown: Binding sites for HSPA9 and HSC20 on ISCU2 are inaccessible when ISCU2 is bound to NFS1-FXN with the core ISC complex. The video was generated on the basis of the cryo-EM structure pdb: 6NZU (10). The HSPA9 binding site (131LPPVK135) is depicted in orange, and the HSC20 binding site (L63, V72, F93) is shown in green (see also Figure 5). The conserved Cys and His residues (sticks and balls) constitute the active center of ISCU2. NFS1 (yellow) and FXN (dark slate grey) are represented as surface model. The HSPA9 binding site is largely occupied by FXN, while the HSC20 binding site is almost fully covered by the C-terminus of NFS1.
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-
111540?utm_source=youtube&utm_medium=bi.lill&utm_campaign=suppvideo
Shown: Binding sites for HSPA9 and HSC20 on ISCU2 are inaccessible when ISCU2 is bound to NFS1-FXN with the core ISC complex. The video was generated on the basis of the cryo-EM structure pdb: 6NZU (10). The HSPA9 binding site (131LPPVK135) is depicted in orange, and the HSC20 binding site (L63, V72, F93) is shown in green (see also Figure 5). The conserved Cys and His residues (sticks and balls) constitute the active center of ISCU2. NFS1 (yellow) and FXN (dark slate grey) are represented as surface model. The HSPA9 binding site is largely occupied by FXN, while the HSC20 binding site is almost fully covered by the C-terminus of NFS1.
