6F5V

Crystal structure of the prephenate aminotransferase from Arabidopsis thaliana

6F5V の概要

• エントリーDOI: 10.2210/pdb6f5v/pdb
• 分子名称: Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase, PYRIDOXAL-5'-PHOSPHATE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: prephenate aminotransferase arabidopsis thaliana, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 205824.62

構造登録者

Cobessi, D.,Robin, A.,Giustini, C.,Graindorge, M.,Matringe, M. (登録日: 2017-12-03, 公開日: 2019-03-13, 最終更新日: 2025-04-09)

主引用文献

Giustini, C.,Graindorge, M.,Cobessi, D.,Crouzy, S.,Robin, A.,Curien, G.,Matringe, M.
Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1 beta aspartate aminotransferase.
Febs J., 286:2118-2134, 2019

PubMed Abstract: Alternative routes for the post-chorismate branch of the biosynthetic pathway leading to tyrosine exist, the 4-hydroxyphenylpyruvate or the arogenate route. The arogenate route involves the transamination of prephenate into arogenate. In a previous study, we found that, depending on the microorganisms possessing the arogenate route, three different aminotransferases evolved to perform prephenate transamination, that is, 1β aspartate aminotransferase (1β AAT), N-succinyl-l,l-diaminopimelate aminotransferase, and branched-chain aminotransferase. The present work aimed at identifying molecular determinant(s) of 1β AAT prephenate aminotransferase (PAT) activity. To that purpose, we conducted X-ray crystal structure analysis of two PAT competent 1β AAT from Arabidopsis thaliana and Rhizobium meliloti and one PAT incompetent 1β AAT from R. meliloti. This structural analysis supported by site-directed mutagenesis, modeling, and molecular dynamics simulations allowed us to identify a molecular determinant of PAT activity in the flexible N-terminal loop of 1β AAT. Our data reveal that a Lys/Arg/Gln residue in position 12 in the sequence (numbering according to Thermus thermophilus 1β AAT), present only in PAT competent enzymes, could interact with the 4-hydroxyl group of the prephenate substrate, and thus may have a central role in the acquisition of PAT activity by 1β AAT.

PubMed: 30771275
DOI: 10.1111/febs.14789

実験手法

X-RAY DIFFRACTION (1.7 Å)