7TDL

M379A mutant tyrosine phenol-lyase complexed with 3-bromo-DL-phenylalanine

7TDL の概要

• エントリーDOI: 10.2210/pdb7tdl/pdb
• 分子名称: Tyrosine phenol-lyase, POTASSIUM ION, (4Z)-4-({[(1E)-2-(3-bromophenyl)-1-carboxyethylidene]azaniumyl}methylidene)-2-methyl-5-[(phosphonooxy)methyl]-1,4-dihydropyridin-3-olate, ... (7 entities in total)
• 機能のキーワード: pyridoxal-5'-phosphate, mutation, substrate specificity, lyase
• 由来する生物種: Citrobacter freundii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 208057.68

構造登録者

Phillips, R.S. (登録日: 2022-01-01, 公開日: 2022-06-01, 最終更新日: 2023-10-18)

主引用文献

Phillips, R.S.,Jones, B.,Nash, S.
M379A Mutant Tyrosine Phenol-lyase from Citrobacter freundii Has Altered Conformational Dynamics.
Chembiochem, 23:e202200028-e202200028, 2022

PubMed Abstract: The M379A mutant of Citrobacter freundii tyrosine phenol-lyase (TPL) has been prepared. M379A TPL is a robust catalyst to prepare a number of tyrosines substituted at the 3-position with bulky groups that cannot be made with wild type TPL. The three dimensional structures of M379A TPL complexed with L-methionine and 3-bromo-DL-phenylalanine have been determined by X-ray crystallography. Methionine is bound as a quinonoid complex in a closed active site in 3 of 4 chains of homotetrameric M379A TPL. M379A TPL reacts with L-methionine about 8-fold slower than wild type TPL. The temperature dependence shows that the slower reaction is due to less positive activation entropy. The structure of the M379A TPL complex of 3-bromo-DL-phenylalanine has a quinonoid complex in two subunits, with an open active site conformation. The effects of the M379A mutation on TPL suggest that the mutant enzyme has altered the conformational dynamics of the active site.

PubMed: 35577764
DOI: 10.1002/cbic.202200028

実験手法

X-RAY DIFFRACTION (1.6 Å)