3hf3

Old Yellow Enzyme from Thermus scotoductus SA-01

spinqualitylabelsall models 3hf3, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hf3 is a 4 chain structure with sequence from Atcc 51532. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMN, SO4 Related: 3hgj Gene: CrS (ATCC 51532) Activity: NADPH dehydrogenase, with EC number 1.6.99.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Recent characterization of the chromate reductase (CrS) from the thermophile Thermus scotoductus SA-01 revealed this enzyme to be related to the Old Yellow Enzyme (OYE) family. Here, we report the structure of a thermostable OYE homolog in its holoform at 2.2A as well as its complex with p-hydroxybenzaldehyde (pHBA). The enzyme crystallized as octamers with the monomers showing a classical TIM barrel fold which upon dimerization yields the biologically active form of the protein. A sulfate ion is bound above the si-side of the non-covalently bound FMN cofactor in the oxidized solved structure but is displaced upon pHBA binding. The active-site architecture is highly conserved as with other members of this enzyme family. The pHBA in the CrS complex is positioned by hydrogen bonding to the two conserved catalytic-site histidines. The most prominent structural difference between CrS and other OYE homologs is the size of the "capping domain". Thermostabilization of the enzyme is achieved in part through increased proline content within loops and turns as well as increased intersubunit interactions through hydrogen bonding and complex salt bridge networks. CrS is able to reduce the C=C bonds of alpha,beta-unsaturated carbonyl compounds with a preference towards cyclic substrates however no activity was observed towards beta-substituted substrates. Mutational studies have confirmed the role of Tyr177 as the proposed proton donor although reduction could still occur at a reduced rate when this residue was mutated to phenylalanine. Crystal structure of a thermostable old yellow enzyme from Thermus scotoductus SA-01.,Opperman DJ, Sewell BT, Litthauer D, Isupov MN, Littlechild JA, van Heerden E Biochem Biophys Res Commun. 2010 Mar 12;393(3):426-31. Epub 2010 Feb 6. PMID:20138824 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also NADPH dehydrogenase

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