%0 Journal Article
%T Crystal structure of an aspartate aminotransferase Lpg0070 from Legionella pneumophila.
%A Gao Y
%A Yang X
%A Hua L
%A Wang M
%A Ge Q
%A Wang W
%A Wang N
%A Ma J
%A Ge H
%J Biochem Biophys Res Commun
%V 689
%N 0
%D 2023 12 31
%M 37984176
%F 3.322
%R 10.1016/j.bbrc.2023.149230
%X 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.