Insight into the 3D structure and substrate specificity of previously uncharacterized GNAT superfamily acetyltransferases from pathogenic bacteria

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• 作者：Karolina A. Majorek^a ; ^d ; Tomasz Osinski^a ; ^d ; David T. Tran^b ; Alina Revilla^b ; Wayne F. Anderson^c ; ^d ; Wladek Minor^a ; ^d ; ^{wladek@iwonka.med.virginia.edu} ; Misty L. Kuhn^b ; ^{mkuhn@sfsu.edu}
• 关键词：Acetyltransferase ; Gcn5-related N-acetyltransferase ; GNAT ; Amino acid acetylation ; Serine and threonine acetylation
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1865
• 期：1
• 页码：55-64
• 全文大小：2473 K
• 卷排序：1865

文摘

We characterized SACOL1063 and CD1211 GNATs of unknown function. SACOL1063 preferentially acetylates the amino acid l-threonine. CD1211 prefers l-Thr, but can also acetylate l-Ser, O-acetyl-l-Ser, and l-Met. The SACOL1063 structure shows substantial conformational changes of an important loop. Two molecules of CoA were bound in donor and acceptor sites of SACOL1063.