Structural insights into the mechanism of Escherichia coli YmdB: A 2′- O -acetyl-ADP-ribose deacetylase
作者: Weichang ZhangChengliang WangYang SongChen ShaoXuan ZhangJianye Zang
作者单位: 1Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People’s Republic of China
2Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230027, People’s Republic of China
3National Synchrotron Radiation Laboratory, University of Science and Technology of China, Hefei, Anhui 230027, People’s Republic of China
刊名: Journal of Structural Biology, 2015, Vol.192 (3), pp.478-486
来源数据库: Elsevier Journal
DOI: 10.1016/j.jsb.2015.10.010
关键词: YmdBDeacetylaseADPrO AADPrMacrodomainCatalytic mechanism
原始语种摘要: Abstract(#br)The Escherichia coli protein YmdB belongs to the macrodomain protein family, which can bind ADP-ribose (ADPr) and its derivatives. Recently, YmdB was reported to be capable of deacetylating O -acetyl-ADP-ribose ( O AADPr) to yield ADPr and free acetate. To study the substrate specificity and catalytic mechanism, the crystal structures of E. coli YmdB in complex with ADPr, double mutant N25AD35A complexed with 2′- O AADPr, and Y126A/ADPr complex were solved at 1.8Å, 2.8Å and 3.0Å resolution, respectively. Structural and biochemical studies reveal that YmdB has substrate specificity against 2′- O AADPr. The conserved residues Asn25 and Asp35 are crucial for catalytic activity, and an active water molecule is proposed as...
全文获取路径: Elsevier  (合作)
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影响因子:3.361 (2012)

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关键词翻译
关键词翻译
  • acetyl 乙酰
  • mechanism 机构
  • Escherichia 埃希氏菌属
  • ribose 核糖
  • ADP Acceptance Data Package