Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB. This paper describes the molecular mechanism of transport of the RND inner membrane component.Įicher, T. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. Sennhauser, G., Amstutz, P., Briand, C., Storchenegger, O. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump. Crystal structure of bacterial multidrug efflux transporter AcrB.

Murakami, S., Nakashima, R., Yamashita, E. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Murakami, S., Nakashima, R., Yamashita, E., Matsumoto, T. This article describes the molecular mechanism of ABC transporters. Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states. coli methionine ABC transporter: structure and allosteric regulation. Multidrug-resistance efflux pumps - not just for resistance. Type I secretion systems - a story of appendices. Two-step and one-step secretion mechanisms in Gram-negative bacteria: contrasting the type IV secretion system and the chaperone–usher pathway of pilus biogenesis. The twin-arginine translocation (Tat) protein export pathway. The bacterial Sec-translocase: structure and mechanism.

Protein secretion systems and adhesins: the molecular armory of Gram-negative pathogens. Recent structural and molecular advances have uncovered remarkable structural and functional similarities between secretion systems that have the potential to be exploited for the development of novel antibacterial compounds. These systems can transport folded or unfolded substrates and use various energy sources to power transport, from ATP to proton or entropy gradients. Double-membrane-spanning secretion systems are composed of many tens of protein subunits and can reach multi-megadalton sizes, whereas outer-membrane-spanning systems are relatively simple and are usually composed of only one type of subunit. These systems are remarkably varied in size, composition and architecture. In this Review, we describe insights into the structural and mechanistic features of the six secretion systems (types I–VI) of Gram-negative bacteria, the unique mycobacterial type VII secretion system, the chaperone–usher pathway and the curli biogenesis machinery. Gram-negative bacteria have evolved a wide array of secretion systems to transport small molecules, proteins and DNA into the extracellular space or target cells.

Gram negative and positive bacteria