2JV7
NMR Solution Structure of Histoplasma capsulatum CBP Homodimer
Summary for 2JV7
| Entry DOI | 10.2210/pdb2jv7/pdb |
| Descriptor | Calcium-binding protein (1 entity in total) |
| Functional Keywords | virulence factor, calcium binding protein, homodimer, all alpha helical, glycoprotein, secreted, metal binding protein |
| Biological source | Ajellomyces capsulatus (Histoplasma capsulatum) |
| Cellular location | Secreted, extracellular space: O42720 |
| Total number of polymer chains | 2 |
| Total formula weight | 15729.44 |
| Authors | Beck, M.R.,DeKoster, G.T.,Cistola, D.P.,Goldman, W.E. (deposition date: 2007-09-12, release date: 2008-09-23, Last modification date: 2024-11-06) |
| Primary citation | Beck, M.R.,Dekoster, G.T.,Cistola, D.P.,Goldman, W.E. NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B. Mol.Microbiol., 72:344-353, 2009 Cited by PubMed Abstract: The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four alpha-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells. PubMed: 19298372DOI: 10.1111/j.1365-2958.2009.06647.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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