Bacterial Periplasmic Binding Protein Tertiary Structures

• Published in: The Journal of biological chemistry Vol. 264; no. 27; pp. 15739 - 15742
• Main Authors: Adams, M D, Oxender, D L
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.09.1989; American Society for Biochemistry and Molecular Biology
• Subjects: Analytical, structural and metabolic biochemistry; Bacterial Proteins; Binding and carrier proteins; Biological and medical sciences; Carrier Proteins; Fundamental and applied biological sciences. Psychology; Gram-Negative Bacteria - metabolism; Models, Structural; Protein Conformation; Proteins; Salmonella typhimurium
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)71535-4

The periplasmic space of Gram-negative bacteria such as Escherichia coli and Salmonella typhimurium contains a large variety of proteins with a wide range of functions. These proteins are associated with nutrient metabolism transport, chemotaxis, antibiotic resistance, and energy utilization. E. coli and S. typhimurium also contain osmotic shock-insensitive permeases which are generally constitutive low affinity systems comprised of a single membrane protein that both recognizes and translocates the substrate from the periplasmic space to the cytosol as well as couples the system to metabolic energy. The osmotic shock-sensitive transport systems are more complex, consisting in each case of at least one soluble periplasmic protein, which is the component for substrate recognition, and two to four inner membrane proteins that play a more direct role in the transfer of the solute across the inner membrane. Reviews of shock-sensitive transport systems describing the genetics and biochemistry of these systems have appeared recently.