5XQA
Crystal Structure of Transketolase in complex with ribose-5-phosphate from Pichia Stipitis
Summary for 5XQA
| Entry DOI | 10.2210/pdb5xqa/pdb |
| Descriptor | Transketolase, THIAMINE DIPHOSPHATE, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | transketolase, transferase |
| Biological source | Scheffersomyces stipitis CBS 6054 (Yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 75749.95 |
| Authors | Li, T.L.,Hsu, N.S.,Wang, Y.L. (deposition date: 2017-06-06, release date: 2018-06-06, 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 Cited by 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: 30155962DOI: 10.1002/cbic.201800378 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.14 Å) |
Structure validation
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