Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/11099
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dc.contributor.authorKaul, Gautam-
dc.contributor.authorPattan, Gurulingappa-
dc.date.accessioned2011-02-25T04:13:07Z-
dc.date.available2011-02-25T04:13:07Z-
dc.date.issued2011-02-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/11099-
dc.description7-13en_US
dc.description.abstractATP-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.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.48(1) [February 2011]en_US
dc.subjectStructureen_US
dc.subjectMsbAen_US
dc.subjectATP-binding cassette transporteren_US
dc.subjectATP hydrolysisen_US
dc.subjectFlip-flopen_US
dc.subjectE. colien_US
dc.titleMsbA ATP-binding cassette (ABC) transporter of E. coli: Structure and possible flippase mechanismen_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.48(1) [February 2011]

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