3V4D

Crystal structure of RutC protein a member of the YjgF family from E.coli

Summary for 3V4D

• Entry DOI: 10.2210/pdb3v4d/pdb
• Descriptor: Aminoacrylate peracid reductase RutC (2 entities in total)
• Functional Keywords: structural genomics, psi-biology, new york structural genomics research consortium, nysgrc, oxidoreductase
• Biological source: Escherichia coli O6
• Total number of polymer chains: 6
• Total formula weight: 87698.54

Authors

Knapik, A.A.,Petkowski, J.J.,Otwinowski, Z.,Cymborowski, M.T.,Cooper, D.R.,Chruszcz, M.,Porebski, P.J.,Niedzialkowska, E.,Almo, S.C.,Minor, W.,New York Structural Genomics Research Consortium (NYSGRC) (deposition date: 2011-12-14, release date: 2012-01-04, Last modification date: 2024-10-09)

Primary citation

Knapik, A.A.,Petkowski, J.J.,Otwinowski, Z.,Cymborowski, M.T.,Cooper, D.R.,Chruszcz, M.,Krajewska, W.M.,Minor, W.
Structure of Escherichia coli RutC, a member of the YjgF family and putative aminoacrylate peracid reductase of the rut operon.
Acta Crystallogr.,Sect.F, 68:1294-1299, 2012

PubMed 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.

PubMed: 23143235
DOI: 10.1107/S1744309112041796

Experimental method

X-RAY DIFFRACTION (1.95 Å)