1ghe
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CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A
OverviewOverview
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.
About this StructureAbout this Structure
1GHE is a Single protein structure of sequence from Pseudomonas syringae pv. tabaci with ACO as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation., He H, Ding Y, Bartlam M, Sun F, Le Y, Qin X, Tang H, Zhang R, Joachimiak A, Liu J, Zhao N, Rao Z, J Mol Biol. 2003 Jan 31;325(5):1019-30. PMID:12527305
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