Unknown

Dataset Information

0

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


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.

SUBMITTER: Knapik AA 

PROVIDER: S-EPMC3515367 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Knapik Aleksandra Alicja AA   Petkowski Janusz Jurand JJ   Otwinowski Zbyszek Z   Cymborowski Marcin Tadeusz MT   Cooper David Robert DR   Chruszcz Maksymilian M   Krajewska Wanda Małgorzata WM   Minor Wladek W  

Acta crystallographica. Section F, Structural biology and crystallization communications 20121026 Pt 11


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  ...[more]

Similar Datasets

| S-EPMC8113886 | biostudies-literature
| S-EPMC1884159 | biostudies-literature
| S-EPMC9638481 | biostudies-literature
| S-EPMC2531270 | biostudies-literature
| S-EPMC5494748 | biostudies-literature
| S-EPMC135098 | biostudies-literature
| S-EPMC177617 | biostudies-other
| S-EPMC107753 | biostudies-literature
| S-EPMC1851613 | biostudies-literature
| S-EPMC3068300 | biostudies-literature