5CE8

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

Summary for 5CE8

• Entry DOI: 10.2210/pdb5ce8/pdb
• Descriptor: Branched-chain amino acid aminotransferase, PYRIDOXAL-5'-PHOSPHATE, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: aminotransferase, branched-chain, plp, bcat, transferase
• Biological source: Thermoproteus uzoniensis (strain 768-20); More
• Total number of polymer chains: 3
• Total formula weight: 103728.37

Authors

Boyko, K.M.,Nikolaeva, A.Y.,Stekhanova, T.N.,Mardanov, A.V.,Rakitin, A.L.,Ravin, N.V.,Popov, V.O. (deposition date: 2015-07-06, release date: 2016-02-24, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)