PMID:22414689

Citation	Kawasaki, K, Kanaba, T, Yoneyama, M, Murata-Kamiya, N, Kojima, C, Ito, Y, Kamiya, H and Mishima, M (2012) Insights into substrate recognition by the Escherichia coli Orf135 protein through its solution structure. Biochem. Biophys. Res. Commun. 420:263-8
Abstract	Escherichia coli Orf135 hydrolyzes oxidatively damaged nucleotides such as 2-hydroxy-dATP, 8-oxo-dGTP and 5-hydroxy-CTP, in addition to 5-methyl-dCTP, dCTP and CTP. Nucleotide pool sanitization by Orf135 is important since nucleotides are continually subjected to potential damage by reactive oxygen species produced during respiration. Orf135 is a member of the Nudix family of proteins which hydrolyze nucleoside diphosphate derivatives. Nudix hydrolases are characterized by the presence of a conserved motif, even though they recognize various substrates and possess a variety of substrate binding pockets. We investigated the tertiary structure of Orf135 and its interaction with a 2-hydroxy-dATP analog using NMR. We report on the solution structure of Orf135, which should contribute towards a structural understanding of Orf135 and its interaction with substrates.
Links	PubMed Online version:10.1016/j.bbrc.2012.02.146
Keywords	Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/chemistry; Amino Acid Motifs; Binding Sites; Escherichia coli/enzymology; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Pyrophosphatases/chemistry; Substrate Specificity
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