View source for 4wws


==Structure of Chlorite dismutase-like Protein from Listeria monocytogenes==
<StructureSection load='4wws' size='340' side='right'caption='[[4wws]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wws]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WWS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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=4wws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wws OCA], [https://pdbe.org/4wws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wws RCSB], [https://www.ebi.ac.uk/pdbsum/4wws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wws ProSAT]</span></td></tr>
</table>
== Function ==
[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:29536725, PubMed:31423350). 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;">
== Publication Abstract from PubMed ==
Chlorite dismutase-like proteins are structurally closely related to functional chlorite dismutases which are heme b-dependent oxidoreductases capable of reducing chlorite to chloride with simultaneous production of dioxygen. Chlorite dismutase-like proteins are incapable of performing this reaction and their biological role is still under discussion. Recently, members of this large protein family were shown to be involved in heme biosynthesis in Gram-positive bacteria, and thus the protein was renamed HemQ in these organisms. In the present work the structural and heme binding properties of the chlorite dismutase-like protein from the Gram-positive pathogen Listeria monocytogenes (LmCld) were analyzed in order to evaluate its potential role as a regulatory heme sensing protein. The homopentameric crystal structure (2.0A) shows high similarity to chlorite-degrading chlorite dismutases with an important difference in the structure of the putative substrate and heme entrance channel. In solution LmCld is a stable hexamer able to bind the low-spin ligand cyanide. Heme binding is reversible with KD-values determined to be 7.2muM (circular dichroism spectroscopy) and 16.8muM (isothermal titration calorimetry) at pH 7.0. Both acidic and alkaline conditions promote heme release. Presented biochemical and structural data reveal that the chlorite dismutase-like protein from L. monocytogenes could act as a potential regulatory heme sensing and storage protein within heme biosynthesis.

Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes.,Hofbauer S, Hagmuller A, Schaffner I, Mlynek G, Krutzler M, Stadlmayr G, Pirker KF, Obinger C, Daims H, Djinovic-Carugo K, Furtmuller PG Arch Biochem Biophys. 2015 Jan 17. pii: S0003-9861(15)00026-0. doi:, 10.1016/j.abb.2015.01.010. PMID:25602700<ref>PMID:25602700</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Listeria monocytogenes EGD-e]]
[[Category: Djinovic-Carugo K]]
[[Category: Hagmueller A]]
[[Category: Mlynek G]]