2DFN
Structure of shikimate kinase from Mycobacterium tuberculosis complexed with ADP and shikimate at 1.9 angstrons of resolution
Summary for 2DFN
| Entry DOI | 10.2210/pdb2dfn/pdb |
| Related | 2DFT |
| Descriptor | Shikimate kinase, CHLORIDE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | alpha/beta, shikimate pathway, transferase |
| Biological source | Mycobacterium tuberculosis |
| Cellular location | Cytoplasm (Probable): P0A4Z2 |
| Total number of polymer chains | 1 |
| Total formula weight | 19249.16 |
| Authors | Dias, M.V.,Faim, L.M.,Vasconcelos, I.B.,de Oliveira, J.S.,Basso, L.A.,Santos, D.S.,de Azevedo, W.F. (deposition date: 2006-03-03, release date: 2006-09-03, Last modification date: 2023-10-25) |
| Primary citation | Dias, M.V.,Faim, L.M.,Vasconcelos, I.B.,de Oliveira, J.S.,Basso, L.A.,Santos, D.S.,de Azevedo, W.F. Effects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosis ACTA CRYSTALLOGR.,SECT.F, 63:1-6, 2007 Cited by PubMed Abstract: Bacteria, fungi and plants can convert carbohydrate and phosphoenolpyruvate into chorismate, which is the precursor of various aromatic compounds. The seven enzymes of the shikimate pathway are responsible for this conversion. Shikimate kinase (SK) is the fifth enzyme in this pathway and converts shikimate to shikimate-3-phosphate. In this work, the conformational changes that occur on binding of shikimate, magnesium and chloride ions to SK from Mycobacterium tuberculosis (MtSK) are described. It was observed that both ions and shikimate influence the conformation of residues of the active site of MtSK. Magnesium influences the conformation of the shikimate hydroxyl groups and the position of the side chains of some of the residues of the active site. Chloride seems to influence the affinity of ADP and its position in the active site and the opening length of the LID domain. Shikimate binding causes a closing of the LID domain and also seems to influence the crystallographic packing of SK. The results shown here could be useful for understanding the catalytic mechanism of SK and the role of ions in the activity of this protein. PubMed: 17183161DOI: 10.1107/S1744309106046823 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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