2JV7

NMR Solution Structure of Histoplasma capsulatum CBP Homodimer

2JV7 の概要

• エントリーDOI: 10.2210/pdb2jv7/pdb
• 分子名称: Calcium-binding protein (1 entity in total)
• 機能のキーワード: virulence factor, calcium binding protein, homodimer, all alpha helical, glycoprotein, secreted, metal binding protein
• 由来する生物種: Ajellomyces capsulatus (Histoplasma capsulatum)
• 細胞内の位置: Secreted, extracellular space: O42720
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15729.44

構造登録者

Beck, M.R.,DeKoster, G.T.,Cistola, D.P.,Goldman, W.E. (登録日: 2007-09-12, 公開日: 2008-09-23, 最終更新日: 2024-11-06)

主引用文献

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

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: 19298372
DOI: 10.1111/j.1365-2958.2009.06647.x

実験手法

SOLUTION NMR