5CE8

Crystal structure of branched-chain aminotransferase from thermophilic archaea Thermoproteus uzoniensis

5CE8 の概要

• エントリーDOI: 10.2210/pdb5ce8/pdb
• 分子名称: Branched-chain amino acid aminotransferase, PYRIDOXAL-5'-PHOSPHATE, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: aminotransferase, branched-chain, plp, bcat, transferase
• 由来する生物種: Thermoproteus uzoniensis (strain 768-20); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 103728.37

構造登録者

Boyko, K.M.,Nikolaeva, A.Y.,Stekhanova, T.N.,Mardanov, A.V.,Rakitin, A.L.,Ravin, N.V.,Popov, V.O. (登録日: 2015-07-06, 公開日: 2016-02-24, 最終更新日: 2024-01-10)

主引用文献

Boyko, K.M.,Stekhanova, T.N.,Nikolaeva, A.Y.,Mardanov, A.V.,Rakitin, A.L.,Ravin, N.V.,Bezsudnova, E.Y.,Popov, V.O.
First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines.
Extremophiles, 20:215-225, 2016

PubMed Abstract: The gene TUZN1299 from the genome of the hyperthermophilic archaeon Thermoproteus uzoniensis encoding a new 32.8 kDa branched-chain amino acid aminotransferase (BCAT) was expressed in Escherichia coli. The recombinant protein TUZN1299 was purified to homogeneity in the PLP-bound form. TUZN1299 was active towards branched-chain amino acids (L-Val, L-Leu, L-Ile) and showed low but detectable activity toward (R)-alpha-methylbenzylamine. The enzyme exhibits high-temperature optimum, thermal stability, and tolerance to organic solvents. The structure of an archaeal BCAT called TUZN1299 was solved for the first time (at 2.0 Å resolution). TUZN1299 has a typical BCAT type IV fold, and the organization of its active site is similar to that of bacterial BCATs. However, there are some differences in the amino acid composition of the active site.

PubMed: 26872794
DOI: 10.1007/s00792-016-0816-z

実験手法

X-RAY DIFFRACTION (2 Å)