5JKQ
Crystal structure of Plasmodium falciparum Pf3D7_0606800 (PfVFT1)
Summary for 5JKQ
| Entry DOI | 10.2210/pdb5jkq/pdb |
| Descriptor | PfVFT1, SULFATE ION (3 entities in total) |
| Functional Keywords | venus fly trap (vft) domain, solute binding protein (sbp), bi-lobed, solute binding protein |
| Biological source | Plasmodium falciparum (isolate 3D7) |
| Total number of polymer chains | 4 |
| Total formula weight | 130565.50 |
| Authors | Parker, M.L.,Boulanger, M.J. (deposition date: 2016-04-26, release date: 2017-07-19, Last modification date: 2024-11-20) |
| Primary citation | Parker, M.L.,Ramaswamy, R.,van Gordon, K.,Powell, C.J.,Bosch, J.,Boulanger, M.J. The structure of Plasmodium falciparum 3D7_0606800 reveals a bi-lobed architecture that supports re-annotation as a Venus Flytrap protein. Protein Sci., 26:1878-1885, 2017 Cited by PubMed Abstract: Plasmodium falciparum, the causative agent of malaria, employs a diverse array of surface displayed proteins to promote dissemination and establish infection in the human host. Of these, Pf3D7_0606800 is highly immunogenic and has been designated a potential top 10 candidate for inclusion in a multicomponent malarial vaccine. The role of Pf3D7_0606800 in parasite biology, however, is unknown and its characterization has been complicated by a lack of sequence identity with proteins of known structure or function. Towards elucidating Pf3D7_0606800 function, we determined its structure to a resolution of 2.35 Å using selenium single wavelength anomalous dispersion. A bi-lobed architecture displays the core structural hallmarks of Venus Flytrap (VFT) proteins prompting us to re-annotate Pf3D7_0606800 as PfVFT1. Structural analysis further revealed an extended inter-lobe groove that, when interrogated by molecular docking, appears well suited to bind peptide-based ligands. Collectively, our structural characterization of the highly antigenic P. falciparum surface protein PfVFT1 provides intriguing functional insight and establishes a structural template that could prove valuable for malaria vaccine engineering studies. PubMed: 28681555DOI: 10.1002/pro.3218 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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