3WWL

Crystal structure of lysine biosynthetic amino acid carrier protein LysW from Thermus thermophilus conjugated with alpha-aminoadipate

3WWL の概要

• エントリーDOI: 10.2210/pdb3wwl/pdb
• 関連するPDBエントリー: 3WWM 3WWN
• 分子名称: Alpha-aminoadipate carrier protein LysW, ZINC ION (3 entities in total)
• 機能のキーワード: zinc finger, amino acid carrier protein, metal binding protein
• 由来する生物種: Thermus thermophilus HB27
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6022.99

構造登録者

Yoshida, A.,Tomita, T.,Kuzuyama, T.,Nishiyama, M. (登録日: 2014-06-21, 公開日: 2014-11-19, 最終更新日: 2023-11-15)

主引用文献

Yoshida, A.,Tomita, T.,Fujimura, T.,Nishiyama, C.,Kuzuyama, T.,Nishiyama, M.
Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ·LysW complex from Thermus thermophilus.
J.Biol.Chem., 290:435-447, 2015

PubMed Abstract: In the biosynthesis of lysine by Thermus thermophilus, the metabolite α-ketoglutarate is converted to the intermediate α-aminoadipate (AAA), which is protected by the 54-amino acid acidic protein LysW. In this study, we determined the crystal structure of LysZ from T. thermophilus (TtLysZ), an amino acid kinase that catalyzes the second step in the AAA to lysine conversion, which was in a complex with LysW at a resolution of 1.85 Å. A crystal analysis coupled with isothermal titration calorimetry of the TtLysZ mutants for TtLysW revealed tight interactions between LysZ and the globular and C-terminal extension domains of the LysW protein, which were mainly attributed to electrostatic forces. These results provided structural evidence for LysW acting as a protecting molecule for the α-amino group of AAA and also as a carrier protein to guarantee better recognition by biosynthetic enzymes for the efficient biosynthesis of lysine.

PubMed: 25392000
DOI: 10.1074/jbc.M114.595983

実験手法

X-RAY DIFFRACTION (1.2 Å)