5dip

Crystal structure of lpg0406 in reduced form from Legionella pneumophila

spinqualitylabelsall models 5dip, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dip is a 2 chain structure with sequence from Legionella pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.097Å Ligands: GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZYG6_LEGPH Publication Abstract from PubMed 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. Structure of lpg0406, a carboxymuconolactone decarboxylase family protein possibly involved in antioxidative response from Legionella pneumophila.,Chen X, Hu Y, Yang B, Gong X, Zhang N, Niu L, Wu Y, Ge H Protein Sci. 2015 Sep 24. doi: 10.1002/pro.2811. PMID:26402328 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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