5zdr

Crystal structure of cyanide-insensitive alternative oxidase from Trypanosoma brucei with ascofuranone derivative

spinqualitylabelsall models 5zdr, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zdr is a 4 chain structure with sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.59Å Ligands: CHW, FE, OH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AOX_TRYBB Catalyzes cyanide-resistant oxygen consumption. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures. Publication Abstract from PubMed The alternative oxidase (AOX) is a monotopic diiron carboxylate protein which catalyzes the four-electron reduction of dioxygen to water by ubiquinol. Although we have recently determined the crystal structure of Trypanosoma brucei AOX (TAO) in the presence and absence of ascofuranone (AF) derivatives (which are potent mixed type inhibitors) the mechanism by which ubiquinol and dioxygen binds to TAO remain inconclusive. In this article, ferulenol was identified as the first competitive inhibitor of AOX which has been used to probe the binding of ubiquinol. Surface plasmon resonance reveals that AF is a quasi-irreversible inhibitor of TAO whilst ferulenol binding is completely reversible. The structure of the TAO-ferulenol complex, determined at 2.7A, provided insights into ubiquinol binding and has also identified a potential dioxygen molecule bound in a side-on conformation to the diiron center for the first time. Insights into the ubiquinol/dioxygen binding and proton relay pathways of the alternative oxidase.,Shiba T, Inaoka DK, Takahashi G, Tsuge C, Kido Y, Young L, Ueda S, Balogun EO, Nara T, Honma T, Tanaka A, Inoue M, Saimoto H, Harada S, Moore AL, Kita K Biochim Biophys Acta Bioenerg. 2019 Mar 22;1860(5):375-382. doi:, 10.1016/j.bbabio.2019.03.008. PMID:30910528 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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