Unknown

Dataset Information

0

Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.


ABSTRACT: P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.93 Å allows detailed structural analyses, including the full organization of an internal hydrogen-bonding network. The orientation of the bound fatty-acid carboxyl group is linked to the protonation states of two coordinating arginine residues. An anion-binding site in the portal region is suggested to be relevant for membrane interactions and conformational changes. When bound to membrane multilayers, P2 has a preferred orientation and is stabilized, and the repeat distance indicates a single layer of P2 between membranes. Simulations show the formation of a double bilayer in the presence of P2, and in cultured cells wild-type P2 induces membrane-domain formation. Here, the most accurate structural and functional view to date on P2, a major component of peripheral nerve myelin, is presented, showing how it can interact with two membranes simultaneously while going through conformational changes at its portal region enabling ligand transfer.

SUBMITTER: Ruskamo S 

PROVIDER: S-EPMC3919267 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.

Ruskamo Salla S   Yadav Ravi P RP   Sharma Satyan S   Lehtimäki Mari M   Laulumaa Saara S   Aggarwal Shweta S   Simons Mikael M   Bürck Jochen J   Ulrich Anne S AS   Juffer André H AH   Kursula Inari I   Kursula Petri P  

Acta crystallographica. Section D, Biological crystallography 20131231 Pt 1


P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.93 Å allows detailed structural analyses, including the full organization of an internal hydrogen-bonding network. The orientation  ...[more]

Similar Datasets

| S-EPMC3515381 | biostudies-literature
| S-EPMC2858655 | biostudies-literature
| S-EPMC5818174 | biostudies-literature
| S-EPMC6345808 | biostudies-literature
| S-EPMC3885250 | biostudies-literature
| S-EPMC3907083 | biostudies-literature
| S-EPMC7016923 | biostudies-literature
| EMPIAR-10424 | biostudies-other
| S-EPMC4466134 | biostudies-literature
| S-EPMC5498104 | biostudies-other