Insights into substrate recognition by the Escherichia coli Orf135 protein through its solution structure

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• 作者：Kumiko Kawasaki^a ; Teppei Kanaba^a ; Momoko Yoneyama^b ; Naoko Murata-Kamiya^c ; Chojiro Kojima^b ; Yutaka Ito^a ; Hiroyuki Kamiya^d ; Masaki Mishima^a ; ^{mishima-masaki@tmu.ac.jp}
• 关键词：NOE ; nuclear Overhauser effect ; NOESY ; NOE spectroscopy ; TOCSY ; total correlation spectroscopy ; HSQC ; heteronuclear single quantum correlation spectroscopy ; r.m.s. ; root mean square
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 出版时间：6 April, 2012
• 年：2012
• 卷：420
• 期：2
• 页码：263-268
• 全文大小：754 K

文摘

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.