5ND5

Crystal structure of transketolase from Chlamydomonas reinhardtii in complex with TPP and Mg2+

Summary for 5ND5

Entry DOI	10.2210/pdb5nd5/pdb
Descriptor	Transketolase, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (4 entities in total)
Functional Keywords	transferase, calvin-benson cycle, thiamine pyrophosphate, magnesium-dependent activation
Biological source	Chlamydomonas reinhardtii
Total number of polymer chains	2
Total formula weight	151432.52
Authors	Fermani, S.,Zaffagnini, M.,Francia, F.,Pasquini, M. (deposition date: 2017-03-07, release date: 2017-06-07, Last modification date: 2024-01-17)
Primary citation	Pasquini, M.,Fermani, S.,Tedesco, D.,Sciabolini, C.,Crozet, P.,Naldi, M.,Henri, J.,Vothknecht, U.,Bertucci, C.,Lemaire, S.D.,Zaffagnini, M.,Francia, F. Structural basis for the magnesium-dependent activation of transketolase from Chlamydomonas reinhardtii. Biochim. Biophys. Acta, 1861:2132-2145, 2017 Cited by PubMed Abstract: In photosynthetic organisms, transketolase (TK) is involved in the Calvin-Benson cycle and participates to the regeneration of ribulose-5-phosphate. Previous studies demonstrated that TK catalysis is strictly dependent on thiamine pyrophosphate (TPP) and divalent ions such as Mg. PubMed: 28552632 DOI: 10.1016/j.bbagen.2017.05.021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.74 Å)

Structure validation