2B5S

Crystal structure of peach Pru p3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens

Summary for 2B5S

• Entry DOI: 10.2210/pdb2b5s/pdb
• Related: 2ALG
• Descriptor: Non-specific lipid transfer protein, LAURIC ACID, HEPTANE, ... (5 entities in total)
• Functional Keywords: non-specific lipid transfer protein, ns-ltp, food allergen, lipid transport
• Biological source: Prunus persica (peach)
• Total number of polymer chains: 2
• Total formula weight: 19162.38

Authors

Pasquato, N.,Berni, R.,Folli, C.,Folloni, S.,Cianci, M.,Pantano, S.,Helliwell, R.J.,Zanotti, G. (deposition date: 2005-09-29, release date: 2005-11-29, Last modification date: 2024-10-30)

Primary citation

Pasquato, N.,Berni, R.,Folli, C.,Folloni, S.,Cianci, M.,Pantano, S.,Helliwell, J.R.,Zanotti, G.
Crystal Structure of Peach Pru p 3, the Prototypic Member of the Family of Plant Non-specific Lipid Transfer Protein Pan-allergens
J.Mol.Biol., 356:684-694, 2006

PubMed Abstract: This study describes the three-dimensional crystal structure of a non-specific lipid transport protein (ns-LTP) from Rosaceae. Whilst ns-LTPs from species other than Rosaceae, such as nuts, cereals, grape, oranges and vegetables are also responsible for plant food allergies, this is less frequent compared with ns-LTPs from Rosaceae in the Mediterranean area. In this heterologously expressed peach Pru p3, a ligand is present inside the central cavity of the protein, presumably a fatty acid that was present or produced in the culture medium of the expression organism Escherichia coli. Moreover, the two molecules of ns-LTP present in the asymmetric unit bind this ligand in a different way, suggesting a significant degree of plasticity for the peach ns-LTP binding cavity, despite the presence of four disulphide bridges. Two molecules are present in the asymmetric unit: molecule A is a fully liganded protein, while molecule B apparently represents a partially liganded state. Also, molecular dynamics simulation, along with other evidence, suggests that these two molecular conformations represent different states in solution. Comparison of the 3D models of different ns-LTPs justifies the evidence of a high degree of conservation of the putative IgE binding epitopes among proteins of the Rosaceae family and the presence of significant amino acid replacements in correspondence of the same regions in ns-LTPs of botanical species unrelated to Rosaceae.

PubMed: 16388823
DOI: 10.1016/j.jmb.2005.11.063

Experimental method

X-RAY DIFFRACTION (2.35 Å)