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==== | ==Cryo-EM structure of the human MCT1 D309N mutant in complex with Basigin-2 in the inward-open conformation.== | ||
<StructureSection load='7da5' size='340' side='right'caption='[[7da5]]' scene=''> | <StructureSection load='7da5' size='340' side='right'caption='[[7da5]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7da5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DA5 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7da5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7da5 OCA], [https://pdbe.org/7da5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7da5 RCSB], [https://www.ebi.ac.uk/pdbsum/7da5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7da5 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7da5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7da5 OCA], [https://pdbe.org/7da5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7da5 RCSB], [https://www.ebi.ac.uk/pdbsum/7da5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7da5 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | |||
[https://www.uniprot.org/uniprot/MOT1_HUMAN MOT1_HUMAN] Metabolic myopathy due to lactate transporter defect;Ketoacidosis due to monocarboxylate transporter-1 deficiency;Exercise-induced hyperinsulinism. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MOT1_HUMAN MOT1_HUMAN] Bidirectional proton-coupled monocarboxylate transporter (PubMed:12946269, PubMed:33333023, PubMed:32946811). Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH (PubMed:12946269, PubMed:33333023). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart (PubMed:32946811). Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 309-Asp is essential for the conformational transition (PubMed:33333023).[UniProtKB:P53986][UniProtKB:P53987]<ref>PMID:12946269</ref> <ref>PMID:32946811</ref> <ref>PMID:33333023</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Jiang X]] | ||
[[Category: Lei J]] | |||
[[Category: Wang N]] | |||
[[Category: Yan C]] | |||
[[Category: Yuan Y]] | |||
[[Category: Zhang S]] | |||
[[Category: Zhu A]] | |||
Latest revision as of 13:53, 27 March 2024
Cryo-EM structure of the human MCT1 D309N mutant in complex with Basigin-2 in the inward-open conformation.Cryo-EM structure of the human MCT1 D309N mutant in complex with Basigin-2 in the inward-open conformation.
Structural highlights
DiseaseMOT1_HUMAN Metabolic myopathy due to lactate transporter defect;Ketoacidosis due to monocarboxylate transporter-1 deficiency;Exercise-induced hyperinsulinism. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. FunctionMOT1_HUMAN Bidirectional proton-coupled monocarboxylate transporter (PubMed:12946269, PubMed:33333023, PubMed:32946811). Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH (PubMed:12946269, PubMed:33333023). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart (PubMed:32946811). Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 309-Asp is essential for the conformational transition (PubMed:33333023).[UniProtKB:P53986][UniProtKB:P53987][1] [2] [3] References
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