8WKJ

The crystal structure of aspartate aminotransferases Lpg0070 from Legionella pneumophila

Summary for 8WKJ

• Entry DOI: 10.2210/pdb8wkj/pdb
• Descriptor: Aminotransferase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: aspartate aminotransferase, legionella pneumophila, transferase
• Biological source: Legionella pneumophila
• Total number of polymer chains: 1
• Total formula weight: 44070.03

Authors

Gao, Y.S.,Hua, L.,Xie, R. (deposition date: 2023-09-27, release date: 2023-12-06)

Primary citation

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., 689:149230-149230, 2023

PubMed Abstract: 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.

PubMed: 37984176
DOI: 10.1016/j.bbrc.2023.149230

Experimental method

X-RAY DIFFRACTION (1.7 Å)