TonB-dependent outer-membrane

The first of the haem uptake systems to be characterized at molecular level was that of Yersinia enterolitica, which closely resembles a typical siderophore uptake system (Stojiljkovic and Hantke, 1992, 1994), including a TonB-dependent outer membrane receptor for haem, a periplasmic binding protein, and a cytoplasmic membrane transport system. There also seems to be a protein that degrades haem and liberates haem iron within the cell. TonB-dependent outer membrane receptor proteins for haem have been cloned and sequenced from Shigella dysenteriae and E. coli (Mills and Payne, 1995 Torres and Payne, 1997), while in Vibrio cholera two genes are required for haem utilization, one an outer membrane receptor a second which may have a TonB-like function (Henderson and Payne, 1994). 

Wiener MC. TonB-dependent outer membrane transport going for Baroque Curr. Opin. Struct. Biol. 2005 15 394-400. 

Specific receptors for siderophores and vitamin B12 have been identified in the OM of Gram-negative bacteria. The translocation of these ligands across the outer membrane follows an energy-dependent mechanism and also involves the TonB, ExbB, ExbD proteins anchored in the cytoplasmic membrane. Biochemical and genetic data indicate that these proteins form a functional unit (the Ton complex), which couples the outer membrane receptor-mediated... 

Figure 1 Examples of several bacterial membrane proteins. The outer membrane (OM) of Gram-negative bacteria contains exclusively fS-barrel proteins, and three examples are shown BtuB (PDB ID 1NQF), which is the 22 p-stranded TonB-dependent active transporter for vitamin B 2/ th LamB or maltoporin trimer (PDB ID 1AF6), which is the 18 p-stranded passive sugar transporter and OmpA (PDB ID 1BXW), which is an 8 p-stranded protein that provides structural support for the OM. Proteins in the cytoplasmic membrane (CM) are helical, and three examples are shown the potassium channel KcsA (PDB ID 1BL8), which is a tetramer Sec YEG (PDB ID 1RH5), which forms the protein transport channel in Methanococcus and BtuCD (PDB ID ...

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