5loq | pdb_00005loq

Structure of coproheme bound HemQ from Listeria monocytogenes

spinqualitylabelsall models 5loq, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5loq is a 5 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 1.69Å Ligands: FEC, MPD, NA 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:31423350, PubMed:29536725). The reaction occurs in a stepwise manner with a three-propionate intermediate (PubMed:27758026, PubMed:31423350). Publication Abstract from PubMed Heme biosynthesis in Gram positive bacteria follows a recently described coproporphyrin-dependent pathway with HemQ catalyzing the decarboxylation of coproheme to heme b. Here we present the first crystal structure of a HemQ (homopentameric coproproheme-HemQ from Listeria monocytogenes) at 1.69 A resolution and the conversion of coproheme to heme b followed by UV-vis and resonance Raman spectroscopy as well as mass spectrometry. The ferric 5-coordinated coproheme iron of HemQ is weakly bound by a neutral proximal histidine H174. In the crystal structure of the resting state the distal Q187 (conserved in Firmicutes HemQ) is H-bonded with propionate p2 and the hydrophobic distal cavity lacks solvent water molecules. Two H2 O2 molecules are shown to be necessary for decarboxylation of the propionates p2 and p4 thereby forming the corresponding vinyl groups of heme b. The overall reaction is relatively slow (kcat /KM = 1.8 x 102 M-1 s-1 at pH 7.0) and occurs in a step-wise manner with a three-propionate intermediate. We present the non-covalent interactions between coproheme and the protein and propose a two-step reaction mechanism. Furthermore, the structure of coproheme-HemQ is compared to that of the phylogenetically related heme b-containing chlorite dismutases. This article is protected by copyright. All rights reserved. Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ - Lessons from the first crystal structure and kinetic studies.,Hofbauer S, Mlynek G, Milazzo L, Puhringer D, Maresch D, Schaffner I, Furtmuller PG, Smulevich G, Djinovic-Carugo K, Obinger C FEBS J. 2016 Oct 18. doi: 10.1111/febs.13930. PMID:27758026 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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