TY - JOUR
T1 - Structural investigation of the proton-coupled secondary transporters
AU - Yan, Nieng
N1 - Funding Information:
This work was supported by funds from the Ministry of Science and Technology (grant numbers 2009CB918802 and 2011CB910501 ), Projects 31125009 and 91017011 of the National Natural Science Foundation of China , and funds from Tsinghua University . Research in Nieng Yan's laboratory was supported in part by an International Early Career Scientist grant from the Howard Hughes Medical Institute .
PY - 2013/8
Y1 - 2013/8
N2 - Transmembrane proton gradients, known as Proton Motive Force (PMF), serve important physiological functions. In addition to driving ATP synthesis, PMF is harnessed by a large variety of secondary transporters to achieve 'uphill' translocation of specific substrates across the membrane. Proton-coupled secondary transporters, including both symporters and antiporters, are widely involved in nutrient uptake and metabolite expulsion, multidrug resistance, and the maintenance of electrolyte homeostasis. Structural studies have led to the identification of several new folds for proton co-transporters, and establish an important framework for the mechanistic understanding of proton-dependent substrate transport. This review focuses on recent advances in the structural elucidation of proton-coupled secondary transporters.
AB - Transmembrane proton gradients, known as Proton Motive Force (PMF), serve important physiological functions. In addition to driving ATP synthesis, PMF is harnessed by a large variety of secondary transporters to achieve 'uphill' translocation of specific substrates across the membrane. Proton-coupled secondary transporters, including both symporters and antiporters, are widely involved in nutrient uptake and metabolite expulsion, multidrug resistance, and the maintenance of electrolyte homeostasis. Structural studies have led to the identification of several new folds for proton co-transporters, and establish an important framework for the mechanistic understanding of proton-dependent substrate transport. This review focuses on recent advances in the structural elucidation of proton-coupled secondary transporters.
UR - http://www.scopus.com/inward/record.url?scp=84881085084&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84881085084&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2013.04.011
DO - 10.1016/j.sbi.2013.04.011
M3 - Review article
C2 - 23806360
AN - SCOPUS:84881085084
SN - 0959-440X
VL - 23
SP - 483
EP - 491
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 4
ER -