Crystal structure of an aspartate aminotransferase Lpg0070 from Legionella pneumophila

Biochem Biophys Res Commun. 2023 Dec 31:689:149230. doi: 10.1016/j.bbrc.2023.149230. Epub 2023 Nov 10.


Legionella pneumophila aspartate aminotransferase (Lpg0070) is a member of the transaminase and belongs to the pyridoxal 5'-phosphate (PLP)-dependent superfamily. It is responsible for the transfer of α-amino between aspartate and α-ketoglutarate to form glutamate and oxaloacetate. Here, we report the crystal structure of Lpg0070 at the resolution of 2.14 Å and 1.7 Å, in apo-form and PLP-bound, respectively. Our structural analysis revealed the specific residues involved in the PLP binding and free form against PLP-bound supported conformational changes before substrate recognition. In vitro enzyme activity proves that the absence of the N-terminal arm reduces the enzyme activity of Lpg0070. These data provide further evidence to support the N-terminal arm plays a crucial role in catalytic activity.

Keywords: Aspartate aminotransferase; Crystal structure; Legionella pneumophila; N-terminal arm.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartate Aminotransferases / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Glutamic Acid / metabolism
  • Legionella pneumophila* / metabolism
  • Models, Molecular
  • Pyridoxal Phosphate / metabolism


  • Aspartate Aminotransferases
  • Pyridoxal Phosphate
  • Glutamic Acid