<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>11</volume><submitter>Hao DL</submitter><pubmed_abstract>AtAMT1;3 is a major contributor to high-affinity ammonium uptake in &lt;i>Arabidopsis&lt;/i> roots. Using a stable electrophysiological recording strategy, we demonstrate in &lt;i>Xenopus laevis&lt;/i> oocytes that AtAMT1;3 functions as a typical high-affinity NH&lt;sub>4&lt;/sub> &lt;sup>+&lt;/sup> uniporter independent of protons and Ca&lt;sup>2+&lt;/sup>. The findings that AtAMT1;3 transports methylammonium (MeA&lt;sup>+&lt;/sup>, a chemical analog of NH&lt;sub>4&lt;/sub> &lt;sup>+&lt;/sup>) with extremely low affinity (&lt;i>K&lt;/i> &lt;sub>m&lt;/sub> in the range of 2.9-6.1 mM) led to investigate the mechanisms underlying substrate binding. Homologous modeling and substrate docking analyses predicted that the deduced substrate binding motif of AtAMT1;3 facilitates the binding of NH&lt;sub>4&lt;/sub> &lt;sup>+&lt;/sup> ions but loosely accommodates the bi</pubmed_abstract><journal>Frontiers in plant science</journal><pagination>571</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7256485</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Functional Characterization of the &lt;i>Arabidopsis&lt;/i> Ammonium Transporter AtAMT1;3 With the Emphasis on Structural Determinants of Substrate Binding and Permeation Properties.</pubmed_title><pmcid>PMC7256485</pmcid><pubmed_authors>Liu SX</pubmed_authors><pubmed_authors>Zhou JY</pubmed_authors><pubmed_authors>Sentenac H</pubmed_authors><pubmed_authors>Hao DL</pubmed_authors><pubmed_authors>Very AA</pubmed_authors><pubmed_authors>Huang YN</pubmed_authors><pubmed_authors>Su YH</pubmed_authors><pubmed_authors>Yang SY</pubmed_authors></additional><is_claimable>false</is_claimable><name>Functional Characterization of the &lt;i>Arabidopsis&lt;/i> Ammonium Transporter AtAMT1;3 With the Emphasis on Structural Determinants of Substrate Binding and Permeation Properties.</name><description>AtAMT1;3 is a major contributor to high-affinity ammonium uptake in &lt;i>Arabidopsis&lt;/i> roots. Using a stable electrophysiological recording strategy, we demonstrate in &lt;i>Xenopus laevis&lt;/i> oocytes that AtAMT1;3 functions as a typical high-affinity NH&lt;sub>4&lt;/sub> &lt;sup>+&lt;/sup> uniporter independent of protons and Ca&lt;sup>2+&lt;/sup>. The findings that AtAMT1;3 transports methylammonium (MeA&lt;sup>+&lt;/sup>, a chemical analog of NH&lt;sub>4&lt;/sub> &lt;sup>+&lt;/sup>) with extremely low affinity (&lt;i>K&lt;/i> &lt;sub>m&lt;/sub> in the range of 2.9-6.1 mM) led to investigate the mechanisms underlying substrate binding. Homologous modeling and substrate docking analyses predicted that the deduced substrate binding motif of AtAMT1;3 facilitates the binding of NH&lt;sub>4&lt;/sub> &lt;sup>+&lt;/sup> ions but loosely accommodates the bi</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020</publication><modification>2026-05-04T12:44:21.435Z</modification><creation>2020-06-14T07:07:04Z</creation></dates><accession>S-EPMC7256485</accession><cross_references><pubmed>32528489</pubmed><doi>10.3389/fpls.2020.00571</doi></cross_references></HashMap>