Structure of Escherichia coli RutC, a member of the YjgF family and putative aminoacrylate peracid reductase of the rut operon

Aleksandra Alicja Knapik, Janusz Jurand Petkowski, Zbyszek Otwinowski, Marcin Tadeusz Cymborowski, David Robert Cooper, Maksymilian Chruszcz, Wanda Małgorzata Krajewska, Wladek Minor

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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 P21212 and contained six molecules in the asymmetric unit. The structure was solved by SAD phasing and was refined to an R work of 19.3% (R free = 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.

Original languageEnglish (US)
Pages (from-to)1294-1299
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number11
DOIs
StatePublished - Nov 2012

Keywords

  • RutC
  • YjgF superfamily
  • aminoacrylate
  • peroxy-aminoacrylate
  • rut operon

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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