2WUT

Crystal structure of human myelin protein P2 in complex with palmitate

Summary for 2WUT

• Entry DOI: 10.2210/pdb2wut/pdb
• Descriptor: MYELIN P2 PROTEIN, PALMITIC ACID, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: myelin, transport, lipid-binding, fatty acid binding protein, peripheral membrane protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm (By similarity): P02689
• Total number of polymer chains: 1
• Total formula weight: 15375.44

Authors

Majava, V.,Nanekar, R.,Kursula, P. (deposition date: 2009-10-09, release date: 2010-05-12, Last modification date: 2023-12-20)

Primary citation

Majava, V.,Polverini, E.,Mazzini, A.,Nanekar, R.,Knoll, W.,Peters, J.,Natali, F.,Baumgartel, P.,Kursula, I.,Kursula, P.
Structural and Functional Characterization of Human Peripheral Nervous System Myelin Protein P2.
Plos One, 5:E300-, 2010

PubMed Abstract: The myelin sheath is a tightly packed multilayered membrane structure insulating selected axons in the central and the peripheral nervous systems. Myelin is a biochemically unique membrane, containing a specific set of proteins. In this study, we expressed and purified recombinant human myelin P2 protein and determined its crystal structure to a resolution of 1.85 A. A fatty acid molecule, modeled as palmitate based on the electron density, was bound inside the barrel-shaped protein. Solution studies using synchrotron radiation indicate that the crystal structure is similar to the structure of the protein in solution. Docking experiments using the high-resolution crystal structure identified cholesterol, one of the most abundant lipids in myelin, as a possible ligand for P2, a hypothesis that was proven by fluorescence spectroscopy. In addition, electrostatic potential surface calculations supported a structural role for P2 inside the myelin membrane. The potential membrane-binding properties of P2 and a peptide derived from its N terminus were studied. Our results provide an enhanced view into the structure and function of the P2 protein from human myelin, which is able to bind both monomeric lipids inside its cavity and membrane surfaces.

PubMed: 20421974
DOI: 10.1371/JOURNAL.PONE.0010300

Experimental method

X-RAY DIFFRACTION (1.85 Å)