Structure and Mechanism of a Na+-Independent Amino Acid Transporter Export

@article{citeulike:5790235, abstract = {Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 angstrom resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of lysine-158 located in a position equivalent to the sodium ion site Na2 of LeuT. We propose that lysine-158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters. 10.1126/science.1176088}, author = {Shaffer, Paul L. and Goehring, April and Shankaranarayanan, Aruna and Gouaux, Eric}, citeulike-article-id = {5790235}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1176088}, citeulike-linkout-1 = {http://www.sciencemag.org/content/325/5943/1010.abstract}, citeulike-linkout-2 = {http://www.sciencemag.org/content/325/5943/1010.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19608859}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19608859}, day = {21}, doi = {10.1126/science.1176088}, issn = {1095-9203}, journal = {Science}, keywords = {imp, ms-13, structure}, month = {August}, number = {5943}, pages = {1010--1014}, posted-at = {2009-11-07 00:02:45}, priority = {2}, title = {Structure and Mechanism of a Na+-Independent Amino Acid Transporter}, url = {http://dx.doi.org/10.1126/science.1176088}, volume = {325}, year = {2009} }

TY - JOUR ID - citeulike:5790235 L3 - citeulike-article-id:5790235 N2 - Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 angstrom resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of lysine-158 located in a position equivalent to the sodium ion site Na2 of LeuT. We propose that lysine-158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters. 10.1126/science.1176088 IS - 5943 JF - Science SN - 1095-9203 EP - 1014 TI - Structure and Mechanism of a Na+-Independent Amino Acid Transporter VL - 325 SP - 1010 KW - imp KW - ms-13 KW - structure AU - Shaffer, Paul AU - Goehring, April AU - Shankaranarayanan, Aruna AU - Gouaux, Eric PY - 2009/08/21/ UR - http://dx.doi.org/10.1126/science.1176088 ER -