About OmpA / Outer Membrane Protein:
Outer membrane proteins are all integrated as forerunners on cytosolic ribosomes. Hydrophobic proteins are guided by molecular chaperones through the cytosol to the mitochondrial surface. Transporting these precursor proteins into the target membrane is specific protein machineries (protein translocases).
Outer Membrane Protein Characteristics
The outer membrane protein has an asymmetrical lipid bilayer, and it is also a highly organized structure. Glycolipid, together with LPS (lipopolysaccharide), is one of the vital components of the outer leaflet. Glycolipid (lipid A) anchors LIPS to the outer membrane.
The outer membrane protein (OmpA) function is to protect the Gram-negative bacteria against a brutal environment, including antibiotics and antimicrobial peptides (AMPs). The outer membrane encloses all the Gram-negative bacteria. While fulfilling its main purpose, it also does numerous functions that are critical to the bacterial cell, like signaling transduction as well as protein and solute translocation. Gram-negative bacteria are firstly enclosed by a thin peptidoglycan cell wall, and then enclosing them all is the outer membrane, which contains lipopolysaccharide.
Outer Membrane Protein Structure
The Outer membrane protein folds into antiparallel beta-barrels and is not like other membrane proteins that consist of transmembrane alpha-helices. It has been determined over recent years that the atomic structure of several outer membrane proteins belongs to six families. They are
●The OmpX protein
●The OmpA membrane domain
●General porins (OmpF, PhoE)
●The TonB-dependent iron siderophore transporters FhuA and FepA
●Substrate-specific porins (LamB, ScrY)