5VIA
Crystal structural of Leishmania major pseudoperoxidase
Summary for 5VIA
| Entry DOI | 10.2210/pdb5via/pdb |
| Descriptor | Pseudoperoxidase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | heme protein, peroxidase, oxidoreductase |
| Biological source | Leishmania major |
| Total number of polymer chains | 1 |
| Total formula weight | 33682.78 |
| Authors | Chreifi, G.,Dejam, D.,Poulos, T.L. (deposition date: 2017-04-14, release date: 2017-06-21, Last modification date: 2024-03-13) |
| Primary citation | Chreifi, G.,Dejam, D.,Poulos, T.L. Crystal structure and functional analysis of Leishmania major pseudoperoxidase. J. Biol. Inorg. Chem., 22:919-927, 2017 Cited by PubMed Abstract: 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-Å 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. PubMed: 28584975DOI: 10.1007/s00775-017-1469-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.764 Å) |
Structure validation
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