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| | ==Structure of coproheme bound HemQ from Listeria monocytogenes== | | ==Structure of coproheme bound HemQ from Listeria monocytogenes== |
| - | <StructureSection load='5loq' size='340' side='right' caption='[[5loq]], [[Resolution|resolution]] 1.69Å' scene=''> | + | <StructureSection load='5loq' size='340' side='right'caption='[[5loq]], [[Resolution|resolution]] 1.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5loq]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LOQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5loq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LOQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FEC:1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC+ACID+FERROUS+COMPLEX'>FEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5loq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loq OCA], [http://pdbe.org/5loq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5loq RCSB], [http://www.ebi.ac.uk/pdbsum/5loq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5loq ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEC:1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC+ACID+FERROUS+COMPLEX'>FEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5loq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loq OCA], [https://pdbe.org/5loq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5loq RCSB], [https://www.ebi.ac.uk/pdbsum/5loq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5loq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Y2113_LISMO Y2113_LISMO]] May function as heme-dependent peroxidase. | + | [https://www.uniprot.org/uniprot/CHDC_LISMO 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).<ref>PMID:27758026</ref> <ref>PMID:29536725</ref> <ref>PMID:31423350</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Djinovic-Carugo, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Hofbauer, S]] | + | [[Category: Listeria monocytogenes]] |
| - | [[Category: Mlynek, G]] | + | [[Category: Djinovic-Carugo K]] |
| - | [[Category: Obinger, C]]
| + | [[Category: Hofbauer S]] |
| - | [[Category: Puehringer, D]]
| + | [[Category: Mlynek G]] |
| - | [[Category: Coproheme]]
| + | [[Category: Obinger C]] |
| - | [[Category: Gram-positive pathogen]]
| + | [[Category: Puehringer D]] |
| - | [[Category: Heme b]] | + | |
| - | [[Category: Heme biosynthesis]] | + | |
| - | [[Category: Hemq]] | + | |
| - | [[Category: Oxidoreductase]] | + | |
| Structural highlights
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).[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hofbauer S, Mlynek G, Milazzo L, Puhringer D, Maresch D, Schaffner I, Furtmuller PG, Smulevich G, Djinovic-Carugo K, Obinger C. Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ - Lessons from the first crystal structure and kinetic studies. FEBS J. 2016 Oct 18. doi: 10.1111/febs.13930. PMID:27758026 doi:http://dx.doi.org/10.1111/febs.13930
- ↑ Milazzo L, Hofbauer S, Howes BD, Gabler T, Furtmüller PG, Obinger C, Smulevich G. Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes. Biochemistry. 2018 Apr 3;57(13):2044-2057. PMID:29536725 doi:10.1021/acs.biochem.8b00186
- ↑ 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. Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme b. ACS Catal. 2019 Aug 2;9(8):6766-6782. doi: 10.1021/acscatal.9b00963. Epub 2019, Jun 18. PMID:31423350 doi:http://dx.doi.org/10.1021/acscatal.9b00963
- ↑ Hofbauer S, Mlynek G, Milazzo L, Puhringer D, Maresch D, Schaffner I, Furtmuller PG, Smulevich G, Djinovic-Carugo K, Obinger C. Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ - Lessons from the first crystal structure and kinetic studies. FEBS J. 2016 Oct 18. doi: 10.1111/febs.13930. PMID:27758026 doi:http://dx.doi.org/10.1111/febs.13930
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