Incorporation of outer membrane protein OmpG in lipid membranes: protein-lipid interactions and beta-barrel orientation.
Biochemistry
; 47(23): 6189-98, 2008 Jun 10.
Article
in En
| MEDLINE
| ID: mdl-18473482
ABSTRACT
OmpG is an intermediate size, monomeric, outer membrane protein from Escherichia coli, with n beta = 14 beta-strands. It has a large pore that is amenable to modification by protein engineering. The stoichiometry ( N b = 20) and selectivity ( K r = 0.7-1.2) of lipid-protein interaction with OmpG incorporated in dimyristoyl phosphatidylcholine bilayer membranes was determined with various 14-position spin-labeled lipids by using EPR spectroscopy. The limited selectivity for different lipid species is consistent with the disposition of charged residues in the protein. The conformation and orientation (beta-strand tilt and beta-barrel order parameters) of OmpG in disaturated phosphatidylcholines of odd and even chain lengths from C(120) to C(170) was determined from polarized infrared spectroscopy of the amide I and amide II bands. A discontinuity in the protein orientation (deduced from the beta-barrel order parameters) is observed at the point of hydrophobic matching of the protein with lipid chain length. Compared with smaller (OmpA; n beta = 8) and larger (FhuA; n beta = 22) monomeric E. coli outer membrane proteins, the stoichiometry of motionally restricted lipids increases linearly with the number of beta-strands, the tilt (beta approximately 44 degrees ) of the beta-strands is comparable for the three proteins, and the order parameter of the beta-barrel increases regularly with n beta. These systematic features of the integration of monomeric beta-barrel proteins in lipid membranes could be useful for characterizing outer membrane proteins of unknown structure.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Outer Membrane Proteins
/
Porins
/
Escherichia coli Proteins
/
Escherichia coli
/
Liposomes
Language:
En
Journal:
Biochemistry
Year:
2008
Document type:
Article
Affiliation country:
Germany