A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport
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Byron C.H. Chu
Abstract
In Escherichia coli the Fhu, Fep and Fec transport systems are involved in the uptake of chelated ferric iron-siderophore complexes, whereas in pathogenic strains heme can also be used as an iron source. An essential step in these pathways is the movement of the ferric-siderophore complex or heme from the outer membrane transporter across the periplasm to the cognate cytoplasmic membrane ATP-dependent transporter. This is accomplished in each case by a dedicated periplasmic binding protein (PBP). Ferric-siderophore binding PBPs belong to the PBP protein superfamily and adopt a bilobal type III structural fold in which the two independently folded amino and carboxy terminal domains are linked together by a single long α-helix of approximately 20 amino acids. Recent structural studies reveal how the PBPs of the Fhu, Fep, Fec and Chu systems are able to bind their corresponding ligands. These complex structures will be discussed and placed in the context of our current understanding of the entire type III family of Gram-negative periplasmic binding proteins and related Gram-positive substrate binding proteins.
©2011 by Walter de Gruyter Berlin New York
Artikel in diesem Heft
- Publisher’s Note
- Publisher’s Note
- Guest Editorial
- Highlight: Membrane transport in light of structure, function, and evolution
- HIGHLIGHT: MEMBRANE TRANSPORT IN LIGHT OF STRUCTURE, FUNCTION, AND EVOLUTION
- Pathways of transport protein evolution: recent advances
- Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts
- Omp85 in eukaryotic systems: one protein family with distinct functions
- Evolution of ABC transporters by gene duplication and their role in human disease
- A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport
- The multidrug transporter Pdr5: a molecular diode?
- The lysosomal polypeptide transporter TAPL: more than a housekeeping factor?
- Pumping lipids with P4-ATPases
- Transporters, Trojan horses and therapeutics: suitability of bile acid and peptide transporters for drug delivery
- Substrate recognition and translocation by polyspecific organic cation transporters
- The ugly side of amphetamines: short- and long-term toxicity of 3,4-methylenedioxymethamphetamine (MDMA, ‘Ecstasy’), methamphetamine and d-amphetamine
- SLC22 transporter family proteins as targets for cytostatic uptake into tumor cells
- Role of the Ca2+-activated Cl- channels bestrophin and anoctamin in epithelial cells
- Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases
- Structure determination of channel and transport proteins by high-resolution microscopy techniques
Artikel in diesem Heft
- Publisher’s Note
- Publisher’s Note
- Guest Editorial
- Highlight: Membrane transport in light of structure, function, and evolution
- HIGHLIGHT: MEMBRANE TRANSPORT IN LIGHT OF STRUCTURE, FUNCTION, AND EVOLUTION
- Pathways of transport protein evolution: recent advances
- Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts
- Omp85 in eukaryotic systems: one protein family with distinct functions
- Evolution of ABC transporters by gene duplication and their role in human disease
- A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport
- The multidrug transporter Pdr5: a molecular diode?
- The lysosomal polypeptide transporter TAPL: more than a housekeeping factor?
- Pumping lipids with P4-ATPases
- Transporters, Trojan horses and therapeutics: suitability of bile acid and peptide transporters for drug delivery
- Substrate recognition and translocation by polyspecific organic cation transporters
- The ugly side of amphetamines: short- and long-term toxicity of 3,4-methylenedioxymethamphetamine (MDMA, ‘Ecstasy’), methamphetamine and d-amphetamine
- SLC22 transporter family proteins as targets for cytostatic uptake into tumor cells
- Role of the Ca2+-activated Cl- channels bestrophin and anoctamin in epithelial cells
- Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases
- Structure determination of channel and transport proteins by high-resolution microscopy techniques
