5XT0

Crystal Structure of Transketolase in complex with TPP intermediate VIII from Pichia Stipitis

5XT0 の概要

• エントリーDOI: 10.2210/pdb5xt0/pdb
• 分子名称: Transketolase, CALCIUM ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: transketolase, transferase
• 由来する生物種: Scheffersomyces stipitis CBS 6054 (Yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76522.82

構造登録者

Li, T.L.,Hsu, N.S.,Wang, Y.L. (登録日: 2017-06-16, 公開日: 2018-06-20, 最終更新日: 2023-11-22)

主引用文献

Hsu, N.S.,Wang, Y.L.,Lin, K.H.,Chang, C.F.,Ke, S.C.,Lyu, S.Y.,Hsu, L.J.,Li, Y.S.,Chen, S.C.,Wang, K.C.,Li, T.L.
Evidence of Diradicals Involved in the Yeast Transketolase Catalyzed Keto-Transferring Reactions.
Chembiochem, 19:2395-2402, 2018

PubMed Abstract: Transketolase (TK) catalyzes a reversible transfer of a two-carbon (C ) unit between phosphoketose donors and phosphoaldose acceptors, for which the group-transfer reaction that follows a one- or two-electron mechanism and the force that breaks the C2"-C3" bond of the ketose donors remain unresolved. Herein, we report ultrahigh-resolution crystal structures of a TK (TKps) from Pichia stipitis in previously undiscovered intermediate states and support a diradical mechanism for a reversible group-transfer reaction. In conjunction with MS, NMR spectroscopy, EPR and computational analyses, it is concluded that the enzyme-catalyzed non-Kekulé diradical cofactor brings about the C2"-C3" bond cleavage/formation for the C -unit transfer reaction, for which suppression of activation energy and activation and destabilization of enzymatic intermediates are facilitated.

PubMed: 30155962
DOI: 10.1002/cbic.201800378

実験手法

X-RAY DIFFRACTION (1.15 Å)