4CHI

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

Summary for 4CHI

• Entry DOI: 10.2210/pdb4chi/pdb
• Descriptor: BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, PHOSPHATE ION, ... (8 entities in total)
• Functional Keywords: transferase
• Biological source: ASPERGILLUS FUMIGATUS
• Total number of polymer chains: 2
• Total formula weight: 75597.29

Authors

Thomsen, M.,Palm, G.J.,Hinrichs, W. (deposition date: 2013-12-02, release date: 2014-04-30, Last modification date: 2025-04-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.27 Å)