1R9J
Transketolase from Leishmania mexicana
Summary for 1R9J
| Entry DOI | 10.2210/pdb1r9j/pdb |
| Descriptor | transketolase, CALCIUM ION, THIAMINE DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | 3 domains, each of the alpha/beta type, thiamine diphosphate binding domain, transferase |
| Biological source | Leishmania mexicana mexicana |
| Total number of polymer chains | 2 |
| Total formula weight | 145338.80 |
| Authors | Veitch, N.J.,Mauger, D.A.,Cazzulo, J.J.,Lindqvist, Y.,Barrett, M.P. (deposition date: 2003-10-30, release date: 2004-11-09, Last modification date: 2023-08-23) |
| Primary citation | Veitch, N.J.,Maugeri, D.A.,Cazzulo, J.J.,Lindqvist, Y.,Barrett, M.P. Transketolase from Leishmania mexicana has a dual subcellular localization. Biochem.J., 382:759-767, 2004 Cited by PubMed Abstract: Transketolase has been characterized in Leishmania mexicana. A gene encoding this enzyme was identified and cloned. The gene was expressed in Escherichia coli and the protein was purified and characterized. An apparent K(m) of 2.75 mM for ribose 5-phosphate was determined. X-ray crystallography was used to determine the three-dimensional structure of the enzyme to a resolution of 2.2 A (1 A identical with 0.1 nm). The C-terminus of the protein contains a type-1 peroxisome-targeting signal, suggestive of a possible glycosomal subcellular localization. Subcellular localization experiments performed with promastigote forms of the parasite revealed that the protein was predominantly cytosolic, although a significant component of the total activity was associated with the glycosomes. Transketolase is thus the first enzyme of the nonoxidative branch of the pentose phosphate pathway whose presence has been demonstrated in a peroxisome-like organelle. PubMed: 15149284DOI: 10.1042/BJ20040459 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.22 Å) |
Structure validation
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