1ZHG
Crystal structure of Beta-Hydroxyacyl-Acyl Carrier Protein Dehydratase (FabZ) from Plasmodium falciparum
Summary for 1ZHG
| Entry DOI | 10.2210/pdb1zhg/pdb |
| Related | 1u1z |
| Descriptor | beta hydroxyacyl-acyl carrier protein dehydratase (2 entities in total) |
| Functional Keywords | fabz, plasmodium falciparum, beta-hydroxyacyl acyl carrier protein dehydratase, hot dog fold, lyase |
| Biological source | Plasmodium falciparum (malaria parasite P. falciparum) |
| Total number of polymer chains | 2 |
| Total formula weight | 30696.15 |
| Authors | Swarnamukhi, P.L.,Sharma, S.K.,Surolia, N.,Surolia, A.,Suguna, K. (deposition date: 2005-04-25, release date: 2006-05-30, Last modification date: 2023-10-25) |
| Primary citation | Swarnamukhi, P.L.,Sharma, S.K.,Bajaj, P.,Surolia, N.,Surolia, A.,Suguna, K. Crystal structure of dimeric FabZ of Plasmodium falciparum reveals conformational switching to active hexamers by peptide flips Febs Lett., 580:2653-2660, 2006 Cited by PubMed Abstract: The crystal structure of beta-hydroxyacyl acyl carrier protein dehydratase of Plasmodium falciparum (PfFabZ) has been determined at a resolution of 2.4 A. PfFabZ has been found to exist as a homodimer (d-PfFabZ) in the crystals of the present study in contrast to the reported hexameric form (h-PfFabZ) which is a trimer of dimers crystallized in a different condition. The catalytic sites of this enzyme are located in deep narrow tunnel-shaped pockets formed at the dimer interface. A histidine residue from one subunit of the dimer and a glutamate residue from the other subunit lining the tunnel form the catalytic dyad in the reported crystal structures. While the position of glutamate remains unaltered in the crystal structure of d-PfFabZ compared to that in h-PfFabZ, the histidine residue takes up an entirely different conformation and moves away from the tunnel leading to a His-Phe cis-trans peptide flip at the histidine residue. In addition, a loop in the vicinity has been observed to undergo a similar flip at a Tyr-Pro peptide bond. These alterations not only prevent the formation of a hexamer but also distort the active site geometry resulting in a dimeric form of FabZ that is incapable of substrate binding. The dimeric state and an altered catalytic site architecture make d-PfFabZ distinctly different from the FabZ structures described so far. Dynamic light scattering and size exclusion chromatographic studies clearly indicate a pH-related switching of the dimers to active hexamers. PubMed: 16643907DOI: 10.1016/j.febslet.2006.04.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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