6J2V

GABA aminotransferase from Corynebacterium glutamicum

6J2V の概要

• エントリーDOI: 10.2210/pdb6j2v/pdb
• 分子名称: PLP-dependent aminotransferases, 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]BUTANOIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Corynebacterium glutamicum ATCC 13032
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 200954.24

構造登録者

Hong, J.,Kim, K.J. (登録日: 2019-01-03, 公開日: 2020-01-15, 最終更新日: 2024-03-27)

主引用文献

Hong, J.,Kim, K.J.
Crystal structure of gamma-aminobutyrate aminotransferase in complex with a PLP-GABA adduct from Corynebacterium glutamicum.
Biochem.Biophys.Res.Commun., 514:601-606, 2019

PubMed Abstract: γ-Aminobutyrate (GABA), a four carbon non-protein amino acid, is used by some microorganisms as a source of carbon and/or nitrogen. Corynebacterium glutamicum has an incomplete GABA shunt that lacks a glutamate decarboxylase coding gene for the conversion of glutamate to GABA. Recently, a novel GABA assimilation system was identified in C. glutamicum. In the cell, GABA aminotransferase (GABA-AT) is the first step of GABA assimilation in the process of utilizing GABA as a carbon and/or nitrogen source. In this study, we report the crystal structure of CgGABA-AT in complex with PLP-GABA. We used structural studies and site-directed mutagenesis experiments to identify the key residues that contribute to the formation of the active site. Furthermore, based on structural comparisons and amino acid sequence alignment, we demonstrate the differences between the GABA-ATs of bacteria, fungi, and animals.

PubMed: 31072617
DOI: 10.1016/j.bbrc.2019.04.194

実験手法

X-RAY DIFFRACTION (1.9 Å)