4CHI

(R)-selective amine transaminase from Aspergillus fumigatus at 1.27 A resolution

4CHI の概要

• エントリーDOI: 10.2210/pdb4chi/pdb
• 分子名称: BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, PHOSPHATE ION, ... (8 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: ASPERGILLUS FUMIGATUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75597.29

構造登録者

Thomsen, M.,Palm, G.J.,Hinrichs, W. (登録日: 2013-12-02, 公開日: 2014-04-30, 最終更新日: 2025-04-09)

主引用文献

Thomsen, M.,Skalden, L.,Palm, G.J.,Hohne, M.,Bornscheuer, U.T.,Hinrichs, W.
Crystallographic Characterization of the (R)-Selective Amine Transaminase from Aspergillus Fumigatus.
Acta Crystallogr.,Sect.D, 70:1086-, 2014

PubMed Abstract: The importance of amine transaminases for producing optically pure chiral precursors for pharmaceuticals and chemicals has substantially increased in recent years. The X-ray crystal structure of the (R)-selective amine transaminase from the fungus Aspergillus fumigatus was solved by S-SAD phasing to 1.84 Å resolution. The refined structure at 1.27 Å resolution provides detailed knowledge about the molecular basis of substrate recognition and conversion to facilitate protein-engineering approaches. The protein forms a homodimer and belongs to fold class IV of the pyridoxal-5'-phosphate-dependent enzymes. Both subunits contribute residues to form two active sites. The structure of the holoenzyme shows the catalytically important cofactor pyridoxal-5'-phosphate bound as an internal aldimine with the catalytically responsible amino-acid residue Lys179, as well as in its free form. A long N-terminal helix is an important feature for the stability of this fungal (R)-selective amine transaminase, but is missing in branched-chain amino-acid aminotransferases and D-amino-acid aminotransferases.

PubMed: 24699652
DOI: 10.1107/S1399004714001084

実験手法

X-RAY DIFFRACTION (1.27 Å)