5u8w | pdb_00005u8w

Dihydrolipoamide dehydrogenase (LpdG) from Pseudomonas aeruginosa bound to NADH

spinqualitylabelsall models 5u8w, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5u8w is a 4 chain structure with sequence from Pseudomonas aeruginosa UCBPP-PA14. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.79Å Ligands: DMS, FAD, NAI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2Z9F5_PSEAB Publication Abstract from PubMed Phenazines are a class of redox-active molecules produced by diverse bacteria and archaea. Many of the biological functions of phenazines, such as mediating signaling, iron acquisition, and redox homeostasis, derive from their redox activity. While prior studies have focused on extracellular phenazine oxidation by oxygen and iron, here we report a search for reductants and catalysts of intracellular phenazine reduction in Pseudomonas aeruginosa Enzymatic assays in cell-free lysate, together with crude fractionation and chemical inhibition, indicate that P. aeruginosa contains multiple enzymes that catalyze the reduction of the endogenous phenazines pyocyanin and phenazine-1-carboxylic acid in both cytosolic and membrane fractions. We used chemical inhibitors to target general enzyme classes and found that an inhibitor of flavoproteins and heme-containing proteins, diphenyleneiodonium, effectively inhibited phenazine reduction in vitro, suggesting that most phenazine reduction derives from these enzymes. Using natively purified proteins, we demonstrate that the pyruvate and alpha-ketoglutarate dehydrogenase complexes directly catalyze phenazine reduction with pyruvate or alpha-ketoglutarate as electron donors. Both complexes transfer electrons to phenazines through the common subunit dihydrolipoamide dehydrogenase, a flavoprotein encoded by the gene lpdG Although we were unable to co-crystalize LpdG with an endogenous phenazine, we report its X-ray crystal structure in the apo form (refined to 1.35 A), bound to NAD+ (1.45 A), and bound to NADH (1.79 A). In contrast to the notion that phenazines support intracellular redox homeostasis by oxidizing NADH, our work suggests that phenazines may substitute for NAD+ in LpdG and other enzymes, achieving the same end by a different mechanism. The pyruvate and alpha-ketoglutarate dehydrogenase complexes of Pseudomonas aeruginosa catalyze pyocyanin and phenazine-1-carboxylic acid reduction via the subunit dihydrolipoamide dehydrogenase.,Glasser NR, Wang BX, Hoy JA, Newman DK J Biol Chem. 2017 Feb 7. pii: jbc.M116.772848. doi: 10.1074/jbc.M116.772848. PMID:28174304 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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