5b3u

Crystal structure of biliverdin reductase in complex with NADP+ from Synechocystis sp. PCC 6803

spinqualitylabelsall models 5b3u, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5b3u is a 2 chain structure with sequence from Synechocystis sp. PCC 6803 substr. Kazusa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.698Å Ligands: NAP, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P72782_SYNY3 Publication Abstract from PubMed Biliverdin reductase catalyses the last step in haem degradation and produces the major lipophilic antioxidant bilirubin via reduction of biliverdin, using NAD(P)H as a cofactor. Despite the importance of biliverdin reductase in maintaining the redox balance, the molecular details of the reaction it catalyses remain unknown. Here we present the crystal structure of biliverdin reductase in complex with biliverdin and NADP+. Unexpectedly, two biliverdin molecules, which we designated the proximal and distal biliverdins, bind with stacked geometry in the active site. The nicotinamide ring of the NADP+ is located close to the reaction site on the proximal biliverdin, supporting that the hydride directly attacks this position of the proximal biliverdin. The results of mutagenesis studies suggest that a conserved Arg185 is essential for the catalysis. The distal biliverdin probably acts as a conduit to deliver the proton from Arg185 to the proximal biliverdin, thus yielding bilirubin. A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity.,Takao H, Hirabayashi K, Nishigaya Y, Kouriki H, Nakaniwa T, Hagiwara Y, Harada J, Sato H, Yamazaki T, Sakakibara Y, Suiko M, Asada Y, Takahashi Y, Yamamoto K, Fukuyama K, Sugishima M, Wada K Nat Commun. 2017 Feb 7;8:14397. doi: 10.1038/ncomms14397. PMID:28169272 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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