2ZYJ
Crystal structure of LysN, alpha-aminoadipate aminotransferase (complexed with N-(5'-phosphopyridoxyl)-L-glutamate), from Thermus thermophilus HB27
2ZYJ の概要
| エントリーDOI | 10.2210/pdb2zyj/pdb |
| 関連するPDBエントリー | 2EGY 2Z1Y 2ZP7 3CBF |
| 分子名称 | Alpha-aminodipate aminotransferase, N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid (3 entities in total) |
| 機能のキーワード | alpha-aminoadipate aminotransferase, thermus thermophilus, aminotransferase, transferase |
| 由来する生物種 | Thermus thermophilus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 88556.02 |
| 構造登録者 | Ouchi, T.,Tomita, T.,Kuzuyama, T.,Nishiyama, M. (登録日: 2009-01-26, 公開日: 2009-09-01, 最終更新日: 2023-11-01) |
| 主引用文献 | 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 Cited by 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: 19632206DOI: 10.1016/j.bbrc.2009.07.096 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.67 Å) |
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