1UC8
Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8
1UC8 の概要
エントリーDOI | 10.2210/pdb1uc8/pdb |
関連するPDBエントリー | 1UC9 |
分子名称 | lysine biosynthesis enzyme (2 entities in total) |
機能のキーワード | lysine biosynthesis, alpha-aminoadipate pathway, riken structural genomics/proteomics initiative, rsgi, structural genomics, biosynthetic protein |
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 | 60878.54 |
構造登録者 | Sakai, H.,Vassylyeva, M.N.,Matsuura, T.,Sekine, S.,Nishiyama, M.,Terada, T.,Shirouzu, M.,Kuramitsu, S.,Vassylyev, D.G.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-04-09, 公開日: 2003-09-23, 最終更新日: 2023-12-27) |
主引用文献 | Sakai, H.,Vassylyeva, M.N.,Matsuura, T.,Sekine, S.,Gotoh, K.,Nishiyama, M.,Terada, T.,Shirouzu, M.,Kuramitsu, S.,Vassylyev, D.G.,Yokoyama, S. Crystal Structure of a Lysine Biosynthesis Enzyme, LysX, from Thermus thermophilus HB8 J.Mol.Biol., 332:729-740, 2003 Cited by PubMed Abstract: The thermophilic bacterium Thermus thermophilus synthesizes lysine through the alpha-aminoadipate pathway, which uses alpha-aminoadipate as a biosynthetic intermediate of lysine. LysX is the essential enzyme in this pathway, and is believed to catalyze the acylation of alpha-aminoadipate. We have determined the crystal structures of LysX and its complex with ADP at 2.0A and 2.38A resolutions, respectively. LysX is composed of three alpha+beta domains, each composed of a four to five-stranded beta-sheet core flanked by alpha-helices. The C-terminal and central domains form an ATP-grasp fold, which is responsible for ATP binding. LysX has two flexible loop regions, which are expected to play an important role in substrate binding and protection. In spite of the low level of sequence identity, the overall fold of LysX is surprisingly similar to that of other ATP-grasp fold proteins, such as D-Ala:D-Ala ligase, PurT-encoded glycinamide ribonucleotide transformylase, glutathione synthetase, and synapsin I. In particular, they share a similar spatial arrangement of the amino acid residues around the ATP-binding site. This observation strongly suggests that LysX is an ATP-utilizing enzyme that shares a common evolutionary ancestor with other ATP-grasp fold proteins possessing a carboxylate-amine/thiol ligase activity. PubMed: 12963379DOI: 10.1016/S0022-2836(03)00946-X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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