5DIP

Crystal structure of lpg0406 in reduced form from Legionella pneumophila

Summary for 5DIP

• Entry DOI: 10.2210/pdb5dip/pdb
• Related: 5DIK
• Descriptor: Alkyl hydroperoxide reductase AhpD, SODIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: alkylhydroperoxidase, oxidoreductase
• Biological source: Legionella pneumophila
• Total number of polymer chains: 2
• Total formula weight: 26815.99

Authors

Chen, X.,Gong, X.,Zhang, N.,Ge, H. (deposition date: 2015-09-01, release date: 2015-10-14, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.097 Å)