4CE5

First crystal structure of an (R)-selective omega-transaminase from Aspergillus terreus

Summary for 4CE5

• Entry DOI: 10.2210/pdb4ce5/pdb
• Descriptor: AT-OMEGATA, PYRIDOXAL-5'-PHOSPHATE, N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-D-GLUTAMIC ACID, ... (6 entities in total)
• Functional Keywords: transferase, aminotransferase, (r)-amine aminotransferase, enantioselectivity, chiral amines, transamination.
• Biological source: ASPERGILLUS TERREUS
• Total number of polymer chains: 2
• Total formula weight: 76204.62

Authors

Lyskowski, A.,Gruber, C.,Steinkellner, G.,Schurmann, M.,Schwab, H.,Gruber, K.,Steiner, K. (deposition date: 2013-11-08, release date: 2014-02-12, Last modification date: 2024-05-01)

Primary citation

Lyskowski, A.,Gruber, C.,Steinkellner, G.,Schurmann, M.,Schwab, H.,Gruber, K.,Steiner, K.
Crystal Structure of an (R)-Selective Omega-Transaminase from Aspergillus Terreus
Plos One, 9:87350-, 2014

PubMed Abstract: Chiral amines are important building blocks for the synthesis of pharmaceutical products, fine chemicals, and agrochemicals. ω-Transaminases are able to directly synthesize enantiopure chiral amines by catalysing the transfer of an amino group from a primary amino donor to a carbonyl acceptor with pyridoxal 5'-phosphate (PLP) as cofactor. In nature, (S)-selective amine transaminases are more abundant than the (R)-selective enzymes, and therefore more information concerning their structures is available. Here, we present the crystal structure of an (R)-ω-transaminase from Aspergillus terreus determined by X-ray crystallography at a resolution of 1.6 Å. The structure of the protein is a homodimer that displays the typical class IV fold of PLP-dependent aminotransferases. The PLP-cofactor observed in the structure is present in two states (i) covalently bound to the active site lysine (the internal aldimine form) and (ii) as substrate/product adduct (the external aldimine form) and free lysine. Docking studies revealed that (R)-transaminases follow a dual binding mode, in which the large binding pocket can harbour the bulky substituent of the amine or ketone substrate and the α-carboxylate of pyruvate or amino acids, and the small binding pocket accommodates the smaller substituent.

PubMed: 24498081
DOI: 10.1371/JOURNAL.PONE.0087350

Experimental method

X-RAY DIFFRACTION (1.63 Å)