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

Journal Article · · Acta Crystallographica. Section A, Foundations of Crystallography

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. This 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%). Moreover, 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.

Research Organization:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI ID:
1057314
Journal Information:
Acta Crystallographica. Section A, Foundations of Crystallography, Vol. 68, Issue (11) ; 11, 2012; ISSN 0108-7673
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
ENGLISH

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