6J2V
GABA aminotransferase from Corynebacterium glutamicum
Summary for 6J2V
| Entry DOI | 10.2210/pdb6j2v/pdb |
| Descriptor | PLP-dependent aminotransferases, 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]BUTANOIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | Corynebacterium glutamicum ATCC 13032 |
| Total number of polymer chains | 4 |
| Total formula weight | 200954.24 |
| Authors | |
| Primary citation | 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 Cited by 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: 31072617DOI: 10.1016/j.bbrc.2019.04.194 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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