7l78

H235C variant of Yeast Ferrochelatase

spinqualitylabelsall models 7l78, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7l78 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CHD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HEMH_YEAST Catalyzes the ferrous insertion into protoporphyrin IX.[HAMAP-Rule:MF_00323] Publication Abstract from PubMed Heme is an essential cofactor required for a plethora of cellular processes in eukaryotes. In metazoans the heme biosynthetic pathway is typically partitioned between the cytosol and mitochondria, with the first and final steps taking place in the mitochondrion. The pathway has been extensively studied and its biosynthetic enzymes structurally characterized to varying extents. Nevertheless, understanding of the regulation of heme synthesis and factors that influence this process in metazoans remains incomplete. Therefore, we investigated the molecular organization as well as the physical and genetic interactions of the terminal pathway enzyme, ferrochelatase (Hem15), in the yeast Saccharomyces cerevisiae. Biochemical and genetic analyses revealed dynamic association of Hem15 with Mic60, a core component of the mitochondrial contact site and cristae organizing system (MICOS). Loss of MICOS negatively impacts Hem15 activity, affects the size of the Hem15 high-mass complex, and results in accumulation of reactive and potentially toxic tetrapyrrole precursors that may cause oxidative damage. Restoring intermembrane connectivity in MICOS-deficient cells mitigates these cytotoxic effects. These data provide new insights into how heme biosynthetic machinery is organized and regulated, linking mitochondrial architecture-organizing factors to heme homeostasis. Mitochondrial contact site and cristae organizing system (MICOS) machinery supports heme biosynthesis by enabling optimal performance of ferrochelatase.,Dietz JV, Willoughby MM, Piel RB 3rd, Ross TA, Bohovych I, Addis HG, Fox JL, Lanzilotta WN, Dailey HA, Wohlschlegel JA, Reddi AR, Medlock AE, Khalimonchuk O Redox Biol. 2021 Oct;46:102125. doi: 10.1016/j.redox.2021.102125. Epub 2021 Sep, 10. PMID:34517185 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferrochelatase 3D structures

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