1TFU
phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis
Summary for 1TFU
| Entry DOI | 10.2210/pdb1tfu/pdb |
| Descriptor | Phosphopantetheine adenylyltransferase (2 entities in total) |
| Functional Keywords | transport protein, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transferase |
| Biological source | Mycobacterium tuberculosis |
| Cellular location | Cytoplasm (By similarity): P0A530 |
| Total number of polymer chains | 1 |
| Total formula weight | 17159.74 |
| Authors | Morris, V.K.,Izard, T.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2004-05-27, release date: 2004-09-14, Last modification date: 2024-02-14) |
| Primary citation | Morris, V.K.,Izard, T. Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase. Protein Sci., 13:2547-2552, 2004 Cited by PubMed Abstract: Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in prokaryotic coenzyme A (CoA) biosynthesis, directing the transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to yield dephospho-CoA (dPCoA). The crystal structures of Escherichia coli PPAT bound to its substrates, product, and inhibitor revealed an allosteric hexameric enzyme with half-of-sites reactivity, and established an in-line displacement catalytic mechanism. To provide insight into the mechanism of ligand binding we solved the apoenzyme (Apo) crystal structure of PPAT from Mycobacterium tuberculosis. In its Apo form, PPAT is a symmetric hexamer with an open solvent channel. However, ligand binding provokes asymmetry and alters the structure of the solvent channel, so that ligand binding becomes restricted to one trimer. PubMed: 15322293DOI: 10.1110/ps.04816904 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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