5via | pdb_00005via

Crystal structural of Leishmania major pseudoperoxidase

spinqualitylabelsall models 5via, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5via is a 1 chain structure with sequence from Leishmania major. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.764Å Ligands: HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4QC30_LEIMA Publication Abstract from PubMed Leishmania major pseudoperoxidase (LmPP) is a recently discovered heme protein expressed by the human pathogen. Previous in vivo and in vitro studies suggest that LmPP is a crucial element of the pathogen's defense mechanism against the reactive nitrogen species peroxynitrite produced during the host immune response. To shed light on the potential mechanism of peroxynitrite detoxification, we have determined the 1.76-A X-ray crystal structure of LmPP, revealing a striking degree of homology with heme peroxidases. The most outstanding structural feature is a Cys/His heme coordination, which corroborates previous spectroscopic and mutagenesis studies. We also used a combination of stopped-flow and electron paramagnetic spectroscopies that together suggest that peroxynitrite is not a substrate for LmPP catalysis, leaving the function of LmPP an open question. Crystal structure and functional analysis of Leishmania major pseudoperoxidase.,Chreifi G, Dejam D, Poulos TL J Biol Inorg Chem. 2017 Aug;22(6):919-927. doi: 10.1007/s00775-017-1469-9. Epub, 2017 Jun 5. PMID:28584975 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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