5flj

enzyme-substrate-dioxygen complex of Ni-quercetinase

spinqualitylabelsall models 5flj, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5flj is a 12 chain structure with sequence from Streptomyces sp. FLA. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.818Å Ligands: DMS, NI, OXY, QUE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A2VA43_9ACTN Publication Abstract from PubMed Quercetin 2,4-dioxygenase (quercetinase) from Streptomyces uses nickel as the active-site cofactor to catalyze oxidative cleavage of the flavonol quercetin. How this unusual active-site metal supports catalysis and O2 activation is under debate. We present crystal structures of Ni-quercetinase in three different states, thus providing direct insight into how quercetin and O2 are activated at the Ni(2+) ion. The Ni(2+) ion is coordinated by three histidine residues and a glutamate residue (E(76) ) in all three states. Upon binding, quercetin replaces one water ligand at Ni and is stabilized by a short hydrogen bond through E(76) , the carboxylate group of which rotates by 90 degrees . This conformational change weakens the interaction between Ni and the remaining water ligand, thereby preparing a coordination site at Ni to bind O2 . O2 binds side-on to the Ni(2+) ion and is perpendicular to the C2-C3 and C3-C4 bonds of quercetin, which are cleaved in the following reaction steps. Quercetin 2,4-Dioxygenase Activates Dioxygen in a Side-On O2 -Ni Complex.,Jeoung JH, Nianios D, Fetzner S, Dobbek H Angew Chem Int Ed Engl. 2016 Mar 1;55(10):3281-4. doi: 10.1002/anie.201510741., Epub 2016 Feb 5. PMID:26846734 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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