Abstract
ABSTRACT The Gcn5-related N-acetyltransferases (GNATs) are widely distributed in living organisms, which catalyze the transfer of the acetyl group from acetyl coenzyme A (AcCoA) to a primary amine. GNATs are involved in important biological processes such as transcriptional activation, hormone synthesis and antibiotic resistance. However, only few bacterial GNATs are well studied thus far, especially for the identification of substrates. The Escherichia coli YjaB protein is a predicted member of the GNAT family, while its biological function remains elusive. To obtain further insights, we determined the high-quality solution structure of apo-form of YjaB (apo-YjaB) by nuclear magnetic resonance (NMR) spectroscopy. The apo-YjaB shows a typical GNAT fold, composing of a central seven-strand E-sheet flanked by four D-helices. In addition, we performed NMR titration experiments to identify the possible AcCoA binding site. The results indicate that YjaB binds with AcCoA in a typical fashion, while subtle structural differences of YjaB with other GNATs suggest that the acceptor specificity may be different. Taken together, our results provide insightful information of the
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