Crystal structure of an aspartate aminotransferase Lpg0070 from Legionella pneumophila

Yongshan Gao; Xiaowen Yang; Lan Hua; Min Wang; Qing Ge; Weiqiang Wang; Na Wang; Jinming Ma; Honghua Ge

doi:10.1016/j.bbrc.2023.149230

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.

Authors

Yongshan Gao¹, Xiaowen Yang², Lan Hua², Min Wang², Qing Ge², Weiqiang Wang², Na Wang², Jinming Ma³, Honghua Ge⁴

Affiliations

¹ Institutes of Material Science and Information Technology, Anhui University, Hefei, 230601, China; School of Resources and Environmental Engineering, Anhui University, Hefei, 230601, China.
² Institutes of Material Science and Information Technology, Anhui University, Hefei, 230601, China.
³ Institutes of Material Science and Information Technology, Anhui University, Hefei, 230601, China. Electronic address: jmma@ahu.edu.cn.
⁴ Institutes of Material Science and Information Technology, Anhui University, Hefei, 230601, China. Electronic address: hhge@ahu.edu.cn.

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

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.

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

Substances

Aspartate Aminotransferases
Pyridoxal Phosphate
Glutamic Acid