TY - JOUR
T1 - ABC transporters
T2 - how small machines do a big job
AU - Davidson, Amy L.
AU - Maloney, Peter C.
N1 - Funding Information:
The authors are grateful to C. Orelle and J. Chen for discussion and G. Lu and M. Oldham for figure preparation. The National Institutes of Health, the National Science Foundation and the Welch Foundation supported work referenced from the authors’ laboratories.
PY - 2007/10
Y1 - 2007/10
N2 - Transporters from the ATP-binding cassette (ABC) superfamily operate in all organisms, from bacteria to humans, to pump substances across biological membranes. Recent high-resolution views of ABC transporters in different conformational states provide clues as to how ATP might be used to drive the structural reorganizations that accompany membrane transport. Importantly, it now appears that a putative translocation pathway running through the center of the transporter might be gated alternately, either at the inside or the outside of the cytoplasmic membrane, coupling substrate translocation to a cycle of ATP-dependent conformational changes. ATP binding and ATP hydrolysis have distinct roles in this cycle: binding favors the outward-facing orientation, whereas hydrolysis returns the transporter to an inward-facing conformation.
AB - Transporters from the ATP-binding cassette (ABC) superfamily operate in all organisms, from bacteria to humans, to pump substances across biological membranes. Recent high-resolution views of ABC transporters in different conformational states provide clues as to how ATP might be used to drive the structural reorganizations that accompany membrane transport. Importantly, it now appears that a putative translocation pathway running through the center of the transporter might be gated alternately, either at the inside or the outside of the cytoplasmic membrane, coupling substrate translocation to a cycle of ATP-dependent conformational changes. ATP binding and ATP hydrolysis have distinct roles in this cycle: binding favors the outward-facing orientation, whereas hydrolysis returns the transporter to an inward-facing conformation.
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U2 - 10.1016/j.tim.2007.09.005
DO - 10.1016/j.tim.2007.09.005
M3 - Review article
C2 - 17920277
AN - SCOPUS:35648963623
SN - 0966-842X
VL - 15
SP - 448
EP - 455
JO - Trends in Microbiology
JF - Trends in Microbiology
IS - 10
ER -