| Literature DB >> 23143235 |
Aleksandra Alicja Knapik1, Janusz Jurand Petkowski, Zbyszek Otwinowski, Marcin Tadeusz Cymborowski, David Robert Cooper, Maksymilian Chruszcz, Wanda Małgorzata Krajewska, Wladek Minor.
Abstract
RutC is the third enzyme in the Escherichia coli rut pathway of uracil degradation. RutC belongs to the highly conserved YjgF family of proteins. The structure of the RutC protein was determined and refined to 1.95 Å resolution. The crystal belonged to space group P2(1)2(1)2 and contained six molecules in the asymmetric unit. The structure was solved by SAD phasing and was refined to an Rwork of 19.3% (Rfree=21.7%). The final model revealed that this protein has a Bacillus chorismate mutase-like fold and forms a homotrimer with a hydrophobic cavity in the center of the structure and ligand-binding clefts between two subunits. A likely function for RutC is the reduction of peroxy-aminoacrylate to aminoacrylate as a part of a detoxification process.Entities:
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Year: 2012 PMID: 23143235 PMCID: PMC3515367 DOI: 10.1107/S1744309112041796
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091