5XT4

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

Summary for 5XT4

• Entry DOI: 10.2210/pdb5xt4/pdb
• Descriptor: Transketolase, CALCIUM ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: transketolase, transferase
• Biological source: Scheffersomyces stipitis CBS 6054 (Yeast)
• Total number of polymer chains: 1
• Total formula weight: 76098.34

Authors

Li, T.L.,Hsu, N.S.,Wang, Y.L. (deposition date: 2017-06-16, release date: 2018-06-20, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.06 Å)