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Crystal structure of a putative n-acetyltransferase (ta0374) from thermoplasma acidophilum
Structural highlights
FunctionPAIA_THEAC Involved in the protection against polyamine toxicity by regulating their concentration. Could also be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. It can use a variety of substrates including spermidine, L-tryptophan, L-leucine, L-lysine, dopamine and tyramine.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGCN5-related N-acetyltransferases (GNATs) are the most widely distributed acetyltransferase systems among all three domains of life. GNATs appear to be involved in several key processes, including microbial antibiotic resistance, compacting eukaryotic DNA, controlling gene expression, and protein synthesis. Here, we report the crystal structure of a putative GNAT Ta0374 from Thermoplasma acidophilum, a hyperacidophilic bacterium, that has been determined in an apo-form, in complex with its natural ligand (acetyl coenzyme A), and in complex with a product of reaction (coenzyme A) obtained by cocrystallization with spermidine. Sequence and structural analysis reveals that Ta0374 belongs to a novel protein family, PaiA, involved in the negative control of sporulation and degradative enzyme production. The crystal structure of Ta0374 confirms that it binds acetyl coenzyme A in a way similar to other GNATs and is capable of acetylating spermidine. Based on structural and docking analysis, it is expected that Glu53 and Tyr93 are key residues for recognizing spermidine. Additionally, we find that the purification His-Tag in the apo-form structure of Ta0374 prevents binding of acetyl coenzyme A in the crystal, though not in solution, and affects a chain-flip rotation of "motif A" which is the most conserved sequence among canonical acetyltransferases. Proteins 2011; (c) 2011 Wiley-Liss, Inc. Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production.,Filippova EV, Shuvalova L, Minasov G, Kiryukhina O, Zhang Y, Clancy S, Radhakrishnan I, Joachimiak A, Anderson WF Proteins. 2011 Aug;79(8):2566-77. doi: 10.1002/prot.23062. Epub 2011 Jun, 1. PMID:21633970[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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