1ITZ
Maize Transketolase in complex with TPP
Summary for 1ITZ
| Entry DOI | 10.2210/pdb1itz/pdb |
| Descriptor | Transketolase, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | calvin cycle, transketolase, zea mays, cofactor, thiamine pyrophosphate, plant, transferase |
| Biological source | Zea mays |
| Cellular location | Plastid, chloroplast thylakoid membrane (By similarity): Q7SIC9 |
| Total number of polymer chains | 3 |
| Total formula weight | 220574.54 |
| Authors | Gerhardt, S.,Echt, S.,Bader, G.,Freigang, J.,Busch, M.,Bacher, A.,Huber, R.,Fischer, M. (deposition date: 2002-02-15, release date: 2003-02-15, Last modification date: 2023-12-27) |
| Primary citation | Gerhardt, S.,Echt, S.,Busch, M.,Freigang, J.,Auerbach, G.,Bader, G.,Martin, W.F.,Bacher, A.,Huber, R.,Fischer, M. Structure and properties of an engineered transketolase from maize PLANT PHYSIOL., 132:1941-1949, 2003 Cited by PubMed Abstract: The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme. PubMed: 12913150DOI: 10.1104/pp.103.020982 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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