1N81
Crystal structure of Pfg27 from Plasmodium falciparum
Summary for 1N81
| Entry DOI | 10.2210/pdb1n81/pdb |
| Descriptor | plasmodium falciparum gamete antigen 27/25 (2 entities in total) |
| Functional Keywords | gametocyte, helical, helix-turn-helix, pxxp, unknown function |
| Biological source | Plasmodium falciparum |
| Total number of polymer chains | 1 |
| Total formula weight | 22520.74 |
| Authors | Sharma, A.,Sharma, I.,Kogkasuriyachai, D.,Kumar, N. (deposition date: 2002-11-19, release date: 2003-03-04, Last modification date: 2024-02-14) |
| Primary citation | Sharma, A.,Sharma, I.,Kogkasuriyachai, D.,Kumar, N. Structure of a gametocyte protein essential for sexual development in Plasmodium falciparum Nat.Struct.Biol., 10:197-203, 2003 Cited by PubMed Abstract: Malaria transmission is dependent on the development of sexual forms of Plasmodium falciparum, called gametocytes, in the vertebrate host. Pfg27 is an abundantly expressed sexual stage-specific protein that is essential for gametocytogenesis in P. falciparum. We describe the crystal structure of Pfg27, which reveals a novel fold composed of two pseudo dyad-related repeats of the helix-turn-helix motif. Structurally equivalent helices of each repeat either form a dimer interface or interact with RNA in vitro. One side of the dimer presents an unprecedented juxtaposition of four polyproline (PXXP) motifs. Preliminary binding data indicate that these sites are capable of binding Src homology-3 (SH3) modules. Molecular modeling suggests that the dimer can accommodate two SH3 modules simultaneously, potentially enabling molecular crosstalk between SH3-containing proteins. The structural and initial biochemical evidence suggests that Pfg27 may serve as a platform for RNA and SH3 binding. PubMed: 12577051DOI: 10.1038/nsb899 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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