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1UC8

Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8

1UC8 の概要
エントリーDOI10.2210/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
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: 12963379
DOI: 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)
構造検証レポート
Validation report summary of 1uc8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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