4jic

Glycerol Trinitrate Reductase NerA from Agrobacterium radiobacter

spinqualitylabelsall models 4jic, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jic is a 3 chain structure with sequence from "achromobacter_radiobacter"_(beijerinck_and_van_delden_1902)_bergey_et_al._1934 "achromobacter radiobacter" (beijerinck and van delden 1902) bergey et al. 1934. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMN, PEG, SO4 Related: 4jip, 4jiq Gene: nerA ("Achromobacter radiobacter" (Beijerinck and van Delden 1902) Bergey et al. 1934) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed In recent years, Old Yellow Enzymes (OYEs) and their homologues have found broad application in the efficient asymmetric hydrogenation of activated CC bonds with high selectivities and yields. Members of this class of enzymes have been found in many different organisms and are rather diverse on the sequence level, with pairwise identities as low as 20 %, but they exhibit significant structural similarities with the adoption of a conserved (alphabeta)8 -barrel fold. Some OYEs have been shown not only to reduce CC double bonds, but also to be capable of reducing nitro groups in both saturated and unsaturated substrates. In order to understand this dual activity we determined and analyzed X-ray crystal structures of NerA from Agrobacterium radiobacter, both in its apo form and in complex with 4-hydroxybenzaldehyde and with 1-nitro-2-phenylpropene. These structures, together with spectroscopic studies of substrate binding to several OYEs, indicate that nitro-containing substrates can bind to OYEs in different binding modes, one of which leads to CC double bond reduction and the other to nitro group reduction. The Structure of Glycerol Trinitrate Reductase NerA from Agrobacterium radiobacter Reveals the Molecular Reason for Nitro- and Ene-Reductase Activity in OYE Homologues.,Oberdorfer G, Binter A, Wallner S, Durchschein K, Hall M, Faber K, Macheroux P, Gruber K Chembiochem. 2013 May 10;14(7):836-45. doi: 10.1002/cbic.201300136. Epub 2013 Apr, 18. PMID:23606302 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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