2ZYJ

Crystal structure of LysN, alpha-aminoadipate aminotransferase (complexed with N-(5'-phosphopyridoxyl)-L-glutamate), from Thermus thermophilus HB27

Summary for 2ZYJ

• Entry DOI: 10.2210/pdb2zyj/pdb
• Related: 2EGY 2Z1Y 2ZP7 3CBF
• Descriptor: Alpha-aminodipate aminotransferase, N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid (3 entities in total)
• Functional Keywords: alpha-aminoadipate aminotransferase, thermus thermophilus, aminotransferase, transferase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 88556.02

Authors

Ouchi, T.,Tomita, T.,Kuzuyama, T.,Nishiyama, M. (deposition date: 2009-01-26, release date: 2009-09-01, Last modification date: 2023-11-01)

Primary citation

Ouchi, T.,Tomita, T.,Miyagawa, T.,Kuzuyama, T.,Nishiyama, M.
Dual roles of a conserved pair, Arg23 and Ser20, in recognition of multiple substrates in alpha-aminoadipate aminotransferase from Thermus thermophilus.
Biochem.Biophys.Res.Commun., 388:21-27, 2009

PubMed Abstract: To clarify the mechanism for substrate recognition of alpha-aminoadipate aminotransferase (AAA-AT) from Thermus thermophilus, the crystal structure of AAA-AT complexed with N-(5'-phosphopyridoxyl)-l-glutamate (PPE) was determined at 1.67 A resolution. The crystal structure revealed that PPE is recognized by amino acid residues the same as those seen in N-(5'-phosphopyridoxyl)-l-alpha-aminoadipate (PPA) recognition; however, to bind the gamma-carboxyl group of Glu at a fixed position, the Calpha atom of the Glu moiety moves 0.80 A toward the gamma-carboxyl group in the PPE complex. Markedly decreased activity for Asp can be explained by the shortness of the aspartyl side chain to be recognized by Arg23 and further dislocation of the Calpha atom of bound Asp. Site-directed mutagenesis revealed that Arg23 has dual functions for reaction, (i) recognition of gamma (delta)-carboxyl group of Glu (AAA) and (ii) rearrangement of alpha2 helix by changing the interacting partners to place the hydrophobic substrate at the suitable position.

PubMed: 19632206
DOI: 10.1016/j.bbrc.2009.07.096

Experimental method

X-RAY DIFFRACTION (1.67 Å)