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

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...

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Bibliographic Details
Published in:Acta crystallographica. Section A, Foundations of crystallography Foundations of crystallography, 2012-11, Vol.68 (11), p.1294-1299
Main Authors: Knapik, Aleksandra Alicja, Petkowski, Janusz Jurand, Otwinowski, Zbyszek, Cymborowski, Marcin Tadeusz, Cooper, David Robert, Chruszcz, Maksymilian, Krajewska, Wanda Małgorzata, Minor, Wladek
Format: Article
Language:English
Subjects:
Amino Acid Sequence
aminoacrylate
Asymmetry
Bacillus
Bacteriology
Catalytic Domain
Conserved Sequence
Crystallography, X-Ray
Crystals
E coli
Enzymes
Escherichia coli
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli Proteins - chemistry
Holes
Hydrogen Bonding
Hydrophobic and Hydrophilic Interactions
Mathematical models
Models, Molecular
Molecular Sequence Annotation
Molecular Sequence Data
Operon
Oxidoreductases - chemistry
Peracids
peroxy-aminoacrylate
Protein Structure, Quaternary
Protein Structure, Secondary
Proteins
rut operon
RutC
Sequence Alignment
Structural Communications
Structural Homology, Protein
Uracil
YjgF superfamily
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Summary: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 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.
ISSN:1744-3091
0108-7673
1744-3091
2053-230X
1600-5724
DOI:10.1107/S1744309112041796