Structural highlights
Function
A0A130QXX8_LEGPN
Publication Abstract from PubMed
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 alpha-amino between aspartate and alpha-ketoglutarate to form glutamate and oxaloacetate. Here, we report the crystal structure of Lpg0070 at the resolution of 2.14 A and 1.7 A, 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.
Crystal structure of an aspartate aminotransferase Lpg0070 from Legionella pneumophila.,Gao Y, Yang X, Hua L, Wang M, Ge Q, Wang W, Wang N, Ma J, Ge H Biochem Biophys Res Commun. 2023 Dec 31;689:149230. doi: , 10.1016/j.bbrc.2023.149230. Epub 2023 Nov 10. PMID:37984176[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gao Y, Yang X, Hua L, Wang M, Ge Q, Wang W, Wang N, Ma J, Ge H. Crystal structure of an aspartate aminotransferase Lpg0070 from Legionella pneumophila. Biochem Biophys Res Commun. 2023 Dec 31;689:149230. PMID:37984176 doi:10.1016/j.bbrc.2023.149230
