3S1V

Transaldolase from Thermoplasma acidophilum in complex with D-fructose 6-phosphate Schiff-base intermediate

3S1V の概要

• エントリーDOI: 10.2210/pdb3s1v/pdb
• 関連するPDBエントリー: 3S0C 3S1U 3S1W 3S1X
• 分子名称: Probable transaldolase, GLYCEROL, FRUCTOSE -6-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: alpha-beta barrel, conformational selection, domain swapping, transferase
• 由来する生物種: Thermoplasma acidophilum
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 124049.69

構造登録者

Lehwess-Litzmann, A.,Neumann, P.,Parthier, C.,Tittmann, K. (登録日: 2011-05-16, 公開日: 2011-08-24, 最終更新日: 2024-10-30)

主引用文献

Lehwess-Litzmann, A.,Neumann, P.,Parthier, C.,Ludtke, S.,Golbik, R.,Ficner, R.,Tittmann, K.
Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism.
Nat.Chem.Biol., 7:678-684, 2011

PubMed Abstract: We examined the catalytic cycle of transaldolase (TAL) from Thermoplasma acidophilum by cryocrystallography and were able to structurally characterize--for the first time, to our knowledge--different genuine TAL reaction intermediates. These include the Schiff base adducts formed between the catalytic lysine and the donor ketose substrates fructose-6-phosphate and sedoheptulose-7-phosphate as well as the Michaelis complex with acceptor aldose erythrose-4-phosphate. These structural snapshots necessitate a revision of the accepted reaction mechanism with respect to functional roles of active site residues, and they further reveal fundamental insights into the general structural features of enzymatic Schiff base intermediates and the role of conformational dynamics in enzyme catalysis, substrate binding and discrimination. A nonplanar arrangement of the substituents around the Schiff base double bond was observed, suggesting that a structurally encoded reactant-state destabilization is a driving force of catalysis. Protein dynamics and the intrinsic hydrogen-bonding pattern appear to be crucial for selective recognition and binding of ketose as first substrate.

PubMed: 21857661
DOI: 10.1038/nchembio.633

実験手法

X-RAY DIFFRACTION (1.8 Å)