5VIA

Crystal structural of Leishmania major pseudoperoxidase

5VIA の概要

• エントリーDOI: 10.2210/pdb5via/pdb
• 分子名称: Pseudoperoxidase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: heme protein, peroxidase, oxidoreductase
• 由来する生物種: Leishmania major
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33682.78

構造登録者

Chreifi, G.,Dejam, D.,Poulos, T.L. (登録日: 2017-04-14, 公開日: 2017-06-21, 最終更新日: 2024-03-13)

主引用文献

Chreifi, G.,Dejam, D.,Poulos, T.L.
Crystal structure and functional analysis of Leishmania major pseudoperoxidase.
J. Biol. Inorg. Chem., 22:919-927, 2017

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: 28584975
DOI: 10.1007/s00775-017-1469-9

実験手法

X-RAY DIFFRACTION (1.764 Å)