Lipoprotein

Lipoprotein

Lipoprotein - Lipoprotein exists in the free form as well as in the bound form (to peptidoglycan with covalent linkage) in the outer membrane.

There are about twice as much bound-form molecules as free-form molecules in E. coli. Lipoprotein has a molecular weight of about 7000 and consists of 58 amino acid residues.

The N-terminal portion contains three almost identical adjacent sequences. Hydrophobic amino acid residues show a regular arrangement in an alternating 3 to 4 pattern of hydrophobic residues.

Lipoprotein has a very high α-helical content.

According to one model the matrix proteins and lipoprotein form an interacting complex which contains diffusion pores of channels (DiRienzo et al., 1978).

Three molecules of matrix protein enclose a diffusion pore with a diameter of 1.5 to 2.0 nm. Each matrix protein molecule is stabilized 01 fixed with a lipoprotein complex consisting of three coiled-coil molecules.

Two of these lipoprotein molecules are in the free form, while the third is in the bound form and s linked to the peptidoglycan layer.

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