5DIP

Crystal structure of lpg0406 in reduced form from Legionella pneumophila

5DIP の概要

• エントリーDOI: 10.2210/pdb5dip/pdb
• 関連するPDBエントリー: 5DIK
• 分子名称: Alkyl hydroperoxide reductase AhpD, SODIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: alkylhydroperoxidase, oxidoreductase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26815.99

構造登録者

Chen, X.,Gong, X.,Zhang, N.,Ge, H. (登録日: 2015-09-01, 公開日: 2015-10-14, 最終更新日: 2023-11-08)

主引用文献

Chen, X.,Hu, Y.,Yang, B.,Gong, X.,Zhang, N.,Niu, L.,Wu, Y.,Ge, H.
Structure of lpg0406, a carboxymuconolactone decarboxylase family protein possibly involved in antioxidative response from Legionella pneumophila
Protein Sci., 24:2070-2075, 2015

PubMed Abstract: Lpg0406, a hypothetical protein from Legionella pneumophila, belongs to carboxymuconolactone decarboxylase (CMD) family. We determined the crystal structure of lpg0406 both in its apo and reduced form. The structures reveal that lpg0406 forms a hexamer and have disulfide exchange properties. The protein has an all-helical fold with a conserved thioredoxin-like active site CXXC motif and a proton relay system similar to that of alkylhydroperoxidase from Mycobacterium tuberculosis (MtAhpD), suggesting that lpg0406 might function as an enzyme with peroxidase activity and involved in antioxidant defense. A comparison of the size and the surface topology of the putative substrate-binding region between lpg0406 and MtAhpD indicates that the two enzymes accommodate the different substrate preferences. The structural findings will enhance understanding of the CMD family protein structure and its various functions.

PubMed: 26402328
DOI: 10.1002/pro.2811

実験手法

X-RAY DIFFRACTION (2.097 Å)