2GPT

Crystal structure of Arabidopsis Dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate

2GPT の概要

• エントリーDOI: 10.2210/pdb2gpt/pdb
• 分子名称: 3-dehydroquinate dehydratase/ shikimate 5-dehydrogenase, SULFATE ION, L(+)-TARTARIC ACID, ... (5 entities in total)
• 機能のキーワード: type i dehydroquinate dehydratase, aroe, shikimate dehydrogenase, arabidopsis thaliana, shikimate, tartrate, bifunctional enzyme, oxidoreductase, lyase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• 細胞内の位置: Plastid, chloroplast (Potential): Q9SQT8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57605.32

構造登録者

Singh, S.A.,Christendat, D. (登録日: 2006-04-18, 公開日: 2006-06-06, 最終更新日: 2024-02-14)

主引用文献

Singh, S.A.,Christendat, D.
Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway
Biochemistry, 45:7787-7796, 2006

PubMed Abstract: The bifunctional enzyme dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) catalyzes the dehydration of dehydroquinate to dehydroshikimate and the reduction of dehydroshikimate to shikimate in the shikimate pathway. We report the first crystal structure of Arabidopsis DHQ-SDH with shikimate bound at the SDH site and tartrate at the DHQ site. The interactions observed in the DHQ-tartrate complex reveal a conserved mode for substrate binding between the plant and microbial DHQ dehydratase family of enzymes. The SDH-shikimate complex provides the first direct evidence of the role of active site residues in the catalytic mechanism. Site-directed mutagenesis and mechanistic analysis revealed that Asp 423 and Lys 385 are key catalytic groups and Ser 336 is a key binding group. The arrangement of the two functional domains reveals that the control of metabolic flux through the shikimate pathway is achieved by increasing the effective concentration of dehydroshikimate through the proximity of the two sites.

PubMed: 16784230
DOI: 10.1021/bi060366+

実験手法

X-RAY DIFFRACTION (1.95 Å)