4JE5

Crystal structure of the aromatic aminotransferase Aro8, a putative alpha-aminoadipate aminotransferase in Saccharomyces cerevisiae

Summary for 4JE5

• Entry DOI: 10.2210/pdb4je5/pdb
• Descriptor: Aromatic/aminoadipate aminotransferase 1, PYRIDOXAL-5'-PHOSPHATE, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (6 entities in total)
• Functional Keywords: transferase, aromatic aminotransferase, alpha-aminoadipate aminotransferase, multifunctional enzyme, plp-dependent, pyridoxal phosphate
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasm : P53090 P53090
• Total number of polymer chains: 4
• Total formula weight: 228431.08

Authors

Bulfer, S.L.,Brunzelle, J.S.,Trievel, R.C. (deposition date: 2013-02-26, release date: 2013-09-11, Last modification date: 2017-11-15)

Primary citation

Bulfer, S.L.,Brunzelle, J.S.,Trievel, R.C.
Crystal structure of Saccharomyces cerevisiae Aro8, a putative alpha-aminoadipate aminotransferase.
Protein Sci., 22:1417-1424, 2013

PubMed Abstract: α-Aminoadipate aminotransferase (AAA-AT) catalyzes the amination of 2-oxoadipate to α-aminoadipate in the fourth step of the α-aminoadipate pathway of lysine biosynthesis in fungi. The aromatic aminotransferase Aro8 has recently been identified as an AAA-AT in Saccharomyces cerevisiae. This enzyme displays broad substrate selectivity, utilizing several amino acids and 2-oxo acids as substrates. Here we report the 1.91Å resolution crystal structure of Aro8 and compare it to AAA-AT LysN from Thermus thermophilus and human kynurenine aminotransferase II. Inspection of the active site of Aro8 reveals asymmetric cofactor binding with lysine-pyridoxal-5-phosphate bound within the active site of one subunit in the Aro8 homodimer and pyridoxamine phosphate and a HEPES molecule bound to the other subunit. The HEPES buffer molecule binds within the substrate-binding site of Aro8, yielding insights into the mechanism by which it recognizes multiple substrates and how this recognition differs from other AAA-AT/kynurenine aminotransferases.

PubMed: 23893908
DOI: 10.1002/pro.2315

Experimental method

X-RAY DIFFRACTION (1.909 Å)