Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli.

摘要: A hybrid gene consisting of the ompF promoter, coding regions for signal peptide, and Ala-Glu residue OmpF NH2 terminus region major outer membrane lipoprotein devoid NH2-terminal cysteine was constructed. Escherichia coli carrying cloned produced predicted protein that is same as except diacyl glycerylcysteine at replaced by residue. The localized in periplasmic space a trimer with noncovalent interaction addition to previously known covalent peptidoglycan. These results strongly indicate exists interactions peptidoglycan layer through domain on one side hydrophobic lipid other side. trimeric structure directly demonstrated chemical cross-linking native both cleavable uncleavable reagents. study also revealed between OmpA protein, protein.