Published in
International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 11(68), p. 1294-1299, 2012
DOI: 10.1107/s1744309112041796
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- [www.ncbi.nlm.nih.gov] | PDF
- [europepmc.org] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
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Structure ofEscherichia coliRutC, a member of the YjgF family and putative aminoacrylate peracid reductase of therutoperon
,
Zbyszek Otwinowski,
Marcin Tadeusz Cymborowski,
David Robert Cooper,
Maksymilian Chruszcz ,
Wanda Małgorzata Krajewska,
Wladek Minor
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Abstract
RutC is the third enzyme in theEscherichia coli rutpathway 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 groupP21212 and contained six molecules in the asymmetric unit. The structure was solved by SAD phasing and was refined to anRworkof 19.3% (Rfree= 21.7%). The final model revealed that this protein has aBacilluschorismate 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.