1sny
Carbonyl reductase Sniffer of D. melanogaster
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OverviewOverview
In vivo studies with the fruit-fly Drosophila melanogaster have shown that, the Sniffer protein prevents age-dependent and oxidative stress-induced, neurodegenerative processes. Sniffer is a NADPH-dependent carbonyl, reductase belonging to the enzyme family of short-chain, dehydrogenases/reductases (SDRs). The crystal structure of the homodimeric, Sniffer protein from Drosophila melanogaster in complex with NADP+ has, been determined by multiple-wavelength anomalous dispersion and refined to, a resolution of 1.75 A. The observed fold represents a typical, dinucleotide-binding domain as detected for other SDRs. With respect to, the cofactor-binding site and the region referred to as substrate-binding, loop, the Sniffer protein shows a striking similarity to the porcine, carbonyl reductase (PTCR). This loop, in both Sniffer and PTCR, is, substantially shortened compared to other SDRs. In most enzymes of the SDR, family this loop adopts a well-defined conformation only after substrate, binding and remains disordered in the absence of any bound ligands or even, if only the dinucleotide cofactor is bound. In the structure of the, Sniffer protein, however, the conformation of this loop is well defined, although no substrate is present. Molecular modeling studies provide an, idea of how binding of substrate molecules to Sniffer could possibly, occur.
About this StructureAbout this Structure
1SNY is a Single protein structure of sequence from Drosophila melanogaster with NAP as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into the neuroprotective-acting carbonyl reductase Sniffer of Drosophila melanogaster., Sgraja T, Ulschmid J, Becker K, Schneuwly S, Klebe G, Reuter K, Heine A, J Mol Biol. 2004 Oct 1;342(5):1613-24. PMID:15364585
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