5K2M
Bifunctional LysX/ArgX from Thermococcus kodakarensis with LysW-gamma-AAA
5K2M の概要
| エントリーDOI | 10.2210/pdb5k2m/pdb |
| 関連するPDBエントリー | 3VPB 3VPC 3VPD |
| 分子名称 | RimK-related lysine biosynthesis protein, Probable lysine biosynthesis protein, ADENOSINE-5'-DIPHOSPHATE, ... (9 entities in total) |
| 機能のキーワード | atp-dependent amine/thiol ligase family amino-group carrier protein lysine biosynthesis arginine biosynthesis, biosynthetic protein |
| 由来する生物種 | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) 詳細 |
| タンパク質・核酸の鎖数 | 14 |
| 化学式量合計 | 284703.88 |
| 構造登録者 | |
| 主引用文献 | Yoshida, A.,Tomita, T.,Atomi, H.,Kuzuyama, T.,Nishiyama, M. Lysine Biosynthesis of Thermococcus kodakarensis with the Capacity to Function as an Ornithine Biosynthetic System. J. Biol. Chem., 291:21630-21643, 2016 Cited by PubMed Abstract: We recently discovered a biosynthetic system using a novel amino group carrier protein called LysW for lysine biosynthesis via α-aminoadipate (AAA), and revealed that this system is also utilized in the biosynthesis of arginine by Sulfolobus In the present study, we focused on the biosynthesis of lysine and ornithine in the hyperthermophilic archaeon Thermococcus kodakarensis, and showed that their biosynthesis is accomplished by a single set of metabolic enzymes. We also determined the crystal structure of the LysX family protein from T. kodakarensis, which catalyzes the conjugation of LysW with either AAA or glutamate, in a complex with LysW-γ-AAA. This crystal structure is the first example to show how LysX recognizes AAA as a substrate and provides a structural basis for the bifunctionality of the LysX family protein from T. kodakarensis Based on comparisons with other LysX family proteins, we propose a mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities. PubMed: 27566549DOI: 10.1074/jbc.M116.743021 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.18 Å) |
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