6fxj

Structure of coproheme decarboxylase from Listeria monocytogenes in complex with iron coproporphyrin III

spinqualitylabelsall models 6fxj, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fxj is a 5 chain structure with sequence from Listeria monocytogenes EGD-e. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.79Å Ligands: CL, FEC, NA, POL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CHDC_LISMO Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:27758026, PubMed:31423350). Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (PubMed:27758026, PubMed:29536725, PubMed:31423350). The reaction occurs in a stepwise manner with a three-propionate intermediate (PubMed:27758026, PubMed:31423350). Publication Abstract from PubMed Coproheme decarboxylase (ChdC) catalyzes the last step in the heme biosynthesis pathway of monoderm bacteria with coproheme acting both as redox cofactor and substrate. Hydrogen peroxide mediates the stepwise decarboxylation of propionates 2 and 4 of coproheme. Here we present the crystal structures of coproheme-loaded ChdC from Listeria monocytogenes (LmChdC) and the three-propionate intermediate, for which the propionate at position 2 (p2) has been converted to a vinyl group and is rotated by 90 degrees compared to the coproheme complex structure. Single, double, and triple mutants of LmChdC, in which H-bonding interactions to propionates 2, 4, 6, and 7 were eliminated, allowed us to obtain the assignment of the coproheme propionates by resonance Raman spectroscopy and to follow the H2O2-mediated conversion of coproheme to heme b. Substitution of H2O2 by chlorite allowed us to monitor compound I formation in the inactive Y147H variant which lacks the catalytically essential Y147. This residue was demonstrated to be oxidized during turnover by using the spin-trap 2-methyl-2-nitrosopropane. Based on these findings and the data derived from molecular dynamics simulations of cofactor structures in distinct poses, we propose a reaction mechanism for the stepwise decarboxylation of coproheme that includes a 90 degrees rotation of the intermediate three-propionate redox cofactor. Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme b.,Milazzo L, Gabler T, Puhringer D, Jandova Z, Maresch D, Michlits H, Pfanzagl V, Djinovic-Carugo K, Oostenbrink C, Furtmuller PG, Obinger C, Smulevich G, Hofbauer S ACS Catal. 2019 Aug 2;9(8):6766-6782. doi: 10.1021/acscatal.9b00963. Epub 2019, Jun 18. PMID:31423350 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA