Crystal structure of Pseudomonas aeruginosa N-acetyltransferase PA4534

Sungwook Shin, Jungwoo Choe

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


The GCN5-related N-acetyltransferase (GNAT) superfamily includes a large and diverse group of enzymes that catalyzes the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate. GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. However, functions of many GNATs remain unknown and PA4534 is one of those uncharacterized GNAT proteins from Pseudomonas aeruginosa. To investigate functions of the PA4534, we determined the apo and Ac-CoA bound PA4534 structures. Our structures showed that PA4534 shared common characteristic structures with other GNAT family N-acetyltransferases and contained a potential substrate binding tunnel close to the bound Ac-CoA.

Original languageEnglish
Pages (from-to)236-240
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - 27 May 2017


  • Acetyltransferase
  • GNAT superfamily
  • PA4534


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