9f0g

LmCpfC H182A variant in complex with iron coproporhyrin III

spinqualitylabelsall models 9f0g, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9f0g is a 1 chain structure with sequence from Listeria monocytogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: CA, EDO, FEC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CPFC_LISMO Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:31794133). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:31794133). Publication Abstract from PubMed Iron insertion into porphyrins is an essential step in heme biosynthesis. In the coproporphyrin-dependent pathway, specific to monoderm bacteria, this reaction is catalyzed by the monomeric enzyme coproporphyrin ferrochelatase. In addition to the mechanistic details of the metalation of the porphyrin, the identification of the substrate access channel for ferrous iron to the active site is important to fully understand this enzymatic system. In fact, whether the iron reaches the active site from the distal or the proximal porphyrin side is still under debate. In this study we have thoroughly addressed this question in Listeria monocytogenes coproporphyrin ferrochelatase by X-ray crystallography, steady-state and pre-steady-state imidazole ligand binding studies, together with a detailed spectroscopic characterization using resonance Raman and UV-vis absorption spectroscopies in solution. Analysis of the X-ray structures of coproporphyrin ferrochelatase-coproporphyrin III crystals soaked with ferrous iron shows that iron is present on both sides of the porphyrin. The kinetic and spectroscopic study of imidazole binding to coproporphyrin ferrochelatase‑iron coproporphyrin III clearly indicates the presence of two possible binding sites in this monomeric enzyme that influence each other, which is confirmed by the observed cooperativity at steady-state and a biphasic behavior in the pre-steady-state experiments. The current results are discussed in the context of the entire heme biosynthetic pathway and pave the way for future studies focusing on protein-protein interactions. Entrance channels to coproheme in coproporphyrin ferrochelatase probed by exogenous imidazole binding.,Dali A, Gabler T, Sebastiani F, Furtmuller PG, Becucci M, Hofbauer S, Smulevich G J Inorg Biochem. 2024 Nov;260:112681. doi: 10.1016/j.jinorgbio.2024.112681. Epub , 2024 Jul 30. PMID:39146673 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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