4i2r | pdb_00004i2r

2.15 Angstroms X-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from Pseudomonas fluorescens

spinqualitylabelsall models 4i2r, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4i2r is a 4 chain structure with sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: 6OH, NA, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q83V33_PSEFL Publication Abstract from PubMed Aldehydes are ubiquitous intermediates in metabolic pathways and their innate reactivity can often make them quite unstable. There are several aldehydic intermediates in the metabolic pathway for tryptophan degradation that can decay into neuroactive compounds that have been associated with numerous neurological diseases. An enzyme of this pathway, 2-aminomuconate-6-semialdehyde dehydrogenase, is responsible for 'disarming' the final aldehydic intermediate. Here we show the crystal structures of a bacterial analogue enzyme in five catalytically relevant forms: resting state, one binary and two ternary complexes, and a covalent, thioacyl intermediate. We also report the crystal structures of a tetrahedral, thiohemiacetal intermediate, a thioacyl intermediate and an NAD(+)-bound complex from an active site mutant. These covalent intermediates are characterized by single-crystal and solution-state electronic absorption spectroscopy. The crystal structures reveal that the substrate undergoes an E/Z isomerization at the enzyme active site before an sp(3)-to-sp(2) transition during enzyme-mediated oxidation. Crystallographic and spectroscopic snapshots reveal a dehydrogenase in action.,Huo L, Davis I, Liu F, Andi B, Esaki S, Iwaki H, Hasegawa Y, Orville AM, Liu A Nat Commun. 2015 Jan 7;6:5935. doi: 10.1038/ncomms6935. PMID:25565451 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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