3kru

Crystal Structure of the Thermostable Old Yellow Enzyme from Thermoanaerobacter pseudethanolicus E39

spinqualitylabelsall models 3kru, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kru is a 4 chain structure with sequence from Thermoanaerobacter pseudethanolicus atcc 33223. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, FMN Related: 3krz Gene: Teth39_0012, ZP_00777979 (Thermoanaerobacter pseudethanolicus ATCC 33223) Activity: NADPH dehydrogenase, with EC number 1.6.99.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We report the crystal structure of a thermophilic "ene" reductase (TOYE) isolated from Thermoanaerobacter pseudethanolicus E39. The crystal structure reveals a tetrameric enzyme and an active site that is relatively large compared to most other structurally determined and related Old Yellow Enzymes. The enzyme adopts higher order oligomeric states (octamers and dodecamers) in solution, as revealed by sedimentation velocity and multiangle laser light scattering. Bead modelling indicates that the solution structure is consistent with the basic tetrameric structure observed in crystallographic studies and electron microscopy. TOYE is stable at high temperatures (T(m)>70 degrees C) and shows increased resistance to denaturation in water-miscible organic solvents compared to the mesophilic Old Yellow Enzyme family member, pentaerythritol tetranitrate reductase. TOYE has typical ene-reductase properties of the Old Yellow Enzyme family. There is currently major interest in using Old Yellow Enzyme family members in the preparative biocatalysis of a number of activated alkenes. The increased stability of TOYE in organic solvents is advantageous for biotransformations in which water-miscible organic solvents and biphasic reaction conditions are required to both deliver novel substrates and minimize product racemisation. Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to old yellow enzyme.,Adalbjornsson BV, Toogood HS, Fryszkowska A, Pudney CR, Jowitt TA, Leys D, Scrutton NS Chembiochem. 2010 Jan 25;11(2):197-207. PMID:19943268 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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