5o0t

CRYSTAL STRUCTURE OF TRANS-MEMBRANE DOMAIN OF Cylindrospermum stagnale NADPH-OXIDASE 5 (NOX5)

spinqualitylabelsall models 5o0t, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o0t is a 1 chain structure with sequence from Cylindrospermum stagnale PCC 7417. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: D10, GOL, HEM, LFA, PEG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K9WT99_9NOST Publication Abstract from PubMed NADPH oxidases (NOXs) are the only enzymes exclusively dedicated to reactive oxygen species (ROS) generation. Dysregulation of these polytopic membrane proteins impacts the redox signaling cascades that control cell proliferation and death. We describe the atomic crystal structures of the catalytic flavin adenine dinucleotide (FAD)- and heme-binding domains of Cylindrospermum stagnale NOX5. The two domains form the core subunit that is common to all seven members of the NOX family. The domain structures were then docked in silico to provide a generic model for the NOX family. A linear arrangement of cofactors (NADPH, FAD, and two membrane-embedded heme moieties) injects electrons from the intracellular side across the membrane to a specific oxygen-binding cavity on the extracytoplasmic side. The overall spatial organization of critical interactions is revealed between the intracellular loops on the transmembrane domain and the NADPH-oxidizing dehydrogenase domain. In particular, the C terminus functions as a toggle switch, which affects access of the NADPH substrate to the enzyme. The essence of this mechanistic model is that the regulatory cues conformationally gate NADPH-binding, implicitly providing a handle for activating/deactivating the very first step in the redox chain. Such insight provides a framework to the discovery of much needed drugs that selectively target the distinct members of the NOX family and interfere with ROS signaling. Crystal structures and atomic model of NADPH oxidase.,Magnani F, Nenci S, Millana Fananas E, Ceccon M, Romero E, Fraaije MW, Mattevi A Proc Natl Acad Sci U S A. 2017 Jun 27;114(26):6764-6769. doi:, 10.1073/pnas.1702293114. Epub 2017 Jun 12. PMID:28607049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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