Structure and mechanism of ABC transporter proteins Export

@article{citeulike:1825061, abstract = {ATP-binding cassette (ABC) transporters are ubiquitous membrane proteins that couple the transport of diverse substrates across cellular membranes to the hydrolysis of ATP. The crystal structures of four ABC transporters have recently been determined. They reveal similar arrangements of the conserved ATP-hydrolyzing nucleotide-binding domains, but unrelated architectures of the transmembrane domains, with the notable exception of a common `coupling helix' that is essential for transmitting conformational changes. The structures suggest a mechanism that rationalizes ATP-driven transport: While binding of ATP appears to trigger an outward-facing conformation, dissociation of the hydrolysis products may promote an inward-facing conformation. This basic scheme can, in principle, explain nutrient import by ABC importers and drug extrusion by ABC exporters.}, author = {Hollenstein, Kaspar and Dawson, Roger J. P. and Locher, Kaspar P.}, booktitle = {Membranes / Engineering and design}, citeulike-article-id = {1825061}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.sbi.2007.07.003}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0959440X07001029}, citeulike-linkout-2 = {http://www.sciencedirect.com/science/article/B6VS6-4PHJMH0-2/2/06ae1c7fd1c6a3b2ae06126b7204c481}, doi = {10.1016/j.sbi.2007.07.003}, issn = {0959440X}, journal = {Current Opinion in Structural Biology}, keywords = {abc}, month = {August}, number = {4}, pages = {412--418}, posted-at = {2008-02-08 19:26:16}, priority = {2}, title = {Structure and mechanism of ABC transporter proteins}, url = {http://dx.doi.org/10.1016/j.sbi.2007.07.003}, volume = {17}, year = {2007} }

TY - JOUR ID - citeulike:1825061 L3 - citeulike-article-id:1825061 N2 - ATP-binding cassette (ABC) transporters are ubiquitous membrane proteins that couple the transport of diverse substrates across cellular membranes to the hydrolysis of ATP. The crystal structures of four ABC transporters have recently been determined. They reveal similar arrangements of the conserved ATP-hydrolyzing nucleotide-binding domains, but unrelated architectures of the transmembrane domains, with the notable exception of a common `coupling helix' that is essential for transmitting conformational changes. The structures suggest a mechanism that rationalizes ATP-driven transport: While binding of ATP appears to trigger an outward-facing conformation, dissociation of the hydrolysis products may promote an inward-facing conformation. This basic scheme can, in principle, explain nutrient import by ABC importers and drug extrusion by ABC exporters. IS - 4 JF - Current Opinion in Structural Biology SN - 0959440X EP - 418 TI - Structure and mechanism of ABC transporter proteins VL - 17 T2 - Membranes / Engineering and design SP - 412 KW - abc AU - Hollenstein, Kaspar AU - Dawson, Roger AU - Locher, Kaspar PY - 2007/08// UR - http://dx.doi.org/10.1016/j.sbi.2007.07.003 ER -