| Literature DB >> 12527305 |
Hongzhen He1, Yi Ding, Mark Bartlam, Fei Sun, Yi Le, Xincheng Qin, Hong Tang, Rongguang Zhang, Andrzej Joachimiak, Jinyuan Liu, Nanming Zhao, Zihe Rao.
Abstract
Tabtoxin resistance protein (TTR) is an enzyme that renders tabtoxin-producing pathogens, such as Pseudomonas syringae, tolerant to their own phytotoxins. Here, we report the crystal structure of TTR complexed with its natural cofactor, acetyl coenzyme A (AcCoA), to 1.55A resolution. The binary complex forms a characteristic "V" shape for substrate binding and contains the four motifs conserved in the GCN5-related N-acetyltransferase (GNAT) superfamily, which also includes the histone acetyltransferases (HATs). A single-step mechanism is proposed to explain the function of three conserved residues, Glu92, Asp130 and Tyr141, in catalyzing the acetyl group transfer to its substrate. We also report that TTR possesses HAT activity and suggest an evolutionary relationship between TTR and other GNAT members.Entities:
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Year: 2003 PMID： 12527305 DOI： 10.1016/s0022-2836(02)01284-6
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469