MsbA ATP-binding cassette (ABC) transporter of E. coli: Structure and possible flippase mechanism.
Indian J Biochem Biophys
; 2011 Feb; 48(1): 7-13
Article
in En
| IMSEAR
| ID: sea-135294
ABSTRACT
ATP-binding cassette (ABC) transporters utilize the energy present in cellular ATP to drive the translocation of structurally diverse set of solutes across the membrane barriers of eubacteria, archaebacteria and eukaryotes. In bacteria, these transporters are considered to be important virulence factors because they play role in nutrient uptake and in the secretion of toxins. The advances in structural determination and functional analysis of bacterial transporters have greatly increased our understanding of the mechanism of transport of these ABC transporters. Although progress in the field of structural biology has been made with the prokaryotic family members, it is likely that eukaryotic transporters will utilize the same mechanisms for translocation process. In this review, we summarize the function of the known MsbA ABC transporters in E. coli and mechanistic insights from structural and possible flippase mechanism studies.
Key words
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Index:
IMSEAR
Main subject:
Membrane Transport Proteins
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Bacterial Proteins
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Biological Transport
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Adenosine Triphosphate
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Protein Structure, Tertiary
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Protein Structure, Secondary
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ATP-Binding Cassette Transporters
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Dimerization
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Phospholipid Transfer Proteins
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Escherichia coli
Language:
En
Journal:
Indian J Biochem Biophys
Year:
2011
Type:
Article