2RJI
Malarial EBA-175 region VI crystallographic structure reveals a KIX-like binding interface
Summary for 2RJI
| Entry DOI | 10.2210/pdb2rji/pdb |
| Related | 1sb0 |
| Descriptor | Erythrocyte binding antigen 175, CALCIUM ION (3 entities in total) |
| Functional Keywords | cbp kix, eba-175, plasmodium falciparum, region vi, protein transport, cell invasion |
| Biological source | Plasmodium falciparum (malaria parasite P. falciparum) |
| Total number of polymer chains | 2 |
| Total formula weight | 20060.56 |
| Authors | Withers-Martinez, C.,Blackman, M.J. (deposition date: 2007-10-15, release date: 2007-11-27, Last modification date: 2024-10-16) |
| Primary citation | Withers-Martinez, C.,Haire, L.F.,Hackett, F.,Walker, P.A.,Howell, S.A.,Smerdon, S.J.,Dodson, G.G.,Blackman, M.J. Malarial EBA-175 Region VI Crystallographic Structure Reveals a KIX-Like Binding Interface J.Mol.Biol., 375:773-781, 2008 Cited by PubMed Abstract: The malaria parasite proliferates in the bloodstream of its vertebrate host by invading and replicating within erythrocytes. To achieve successful invasion, a number of discrete and essential events need to take place at the parasite-host cell interface. Erythrocyte-binding antigen 175 (EBA-175) is a member of a family of Plasmodium falciparum erythrocyte-binding proteins involved in the formation of a tight junction, a necessary step in invasion. Here we present the crystal structure of EBA-175 region VI (rVI), a cysteine-rich domain that is highly conserved within the protein family and is essential for EBA-175 trafficking. The structure was solved by selenomethionine single-wavelength anomalous dispersion at 1.8 A resolution. It reveals a homodimer, containing in each subunit a compact five-alpha-helix core that is stabilized by four conserved disulfide bridges. rVI adopts a novel fold that is likely conserved across the protein family, indicating a conserved function. It shows no similarity to the Duffy-binding-like domains of EBA-175 involved in erythrocyte binding, indicating a distinct role. Remarkably, rVI possesses structural features related to the KIX-binding domain of the coactivator CREB-binding protein, supporting the binding and trafficking roles that have been ascribed to it and providing a rational basis for further experimental investigation of its function. PubMed: 18036613DOI: 10.1016/j.jmb.2007.10.071 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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