4WWS

Structure of Chlorite dismutase-like Protein from Listeria monocytogenes

Summary for 4WWS

• Entry DOI: 10.2210/pdb4wws/pdb
• Descriptor: Putative heme-dependent peroxidase lmo2113, POTASSIUM ION (3 entities in total)
• Functional Keywords: ferredoxin-like fold, chlorite dismutase-like protein, oxidoreductase
• Biological source: Listeria monocytogenes serovar 1/2a
• Total number of polymer chains: 5
• Total formula weight: 145249.76

Authors

Hagmueller, A.,Mlynek, G.,Djinovic-Carugo, K. (deposition date: 2014-11-12, release date: 2015-02-04, Last modification date: 2024-07-10)

Primary citation

Hofbauer, S.,Hagmuller, A.,Schaffner, I.,Mlynek, G.,Krutzler, M.,Stadlmayr, G.,Pirker, K.F.,Obinger, C.,Daims, H.,Djinovic-Carugo, K.,Furtmuller, P.G.
Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes.
Arch.Biochem.Biophys., 574:36-48, 2015

PubMed Abstract: 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 (2.0Å) 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 7.2μM (circular dichroism spectroscopy) and 16.8μM (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.

PubMed: 25602700
DOI: 10.1016/j.abb.2015.01.010

Experimental method

X-RAY DIFFRACTION (2 Å)