2jv7
From Proteopedia
NMR Solution Structure of Histoplasma capsulatum CBP Homodimer
Structural highlights
FunctionCBP1_AJECG Involved in calcium binding and uptake in yeast phase. Required for growth in limiting calcium conditions and for yeast survival in host macrophages. Is able to bind a variety of lipids.[1] [2] Publication Abstract from PubMedThe 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. NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B.,Beck MR, Dekoster GT, Cistola DP, Goldman WE Mol Microbiol. 2009 Apr;72(2):344-53. Epub 2009 Mar 3. PMID:19298372[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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