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==Structure of the thermostabilized transmembrane domain of the CorC Mg2+ transporter in complex with Mg2+== | ==Structure of the thermostabilized transmembrane domain of the bacterial CNNM/CorC family Mg2+ transporter in complex with Mg2+== | ||
<StructureSection load='7cff' size='340' side='right'caption='[[7cff]]' scene=''> | <StructureSection load='7cff' size='340' side='right'caption='[[7cff]], [[Resolution|resolution]] 2.00Å' 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=7CFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CFF FirstGlance]. <br> | <table><tr><td colspan='2'>[[7cff]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermus_parvatiensis"_dwivedi_et_al._2015 "thermus parvatiensis" dwivedi et al. 2015]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CFF 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=7cff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cff OCA], [https://pdbe.org/7cff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cff RCSB], [https://www.ebi.ac.uk/pdbsum/7cff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cff ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AV541_07030 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=456163 "Thermus parvatiensis" Dwivedi et al. 2015])</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=7cff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cff OCA], [https://pdbe.org/7cff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cff RCSB], [https://www.ebi.ac.uk/pdbsum/7cff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cff ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The CNNM/CorC family proteins are Mg(2+) transporters that are widely distributed in all domains of life. In bacteria, CorC has been implicated in the survival of pathogenic microorganisms. In humans, CNNM proteins are involved in various biological events, such as body absorption/reabsorption of Mg(2+) and genetic disorders. Here, we determined the crystal structure of the Mg(2+)-bound CorC TM domain dimer. Each protomer has a single Mg(2+) binding site with a fully dehydrated Mg(2+) ion. The residues at the Mg(2+) binding site are strictly conserved in both human CNNM2 and CNNM4, and many of these residues are associated with genetic diseases. Furthermore, we determined the structures of the CorC cytoplasmic region containing its regulatory ATP-binding domain. A combination of structural and functional analyses not only revealed the potential interface between the TM and cytoplasmic domains but also showed that ATP binding is important for the Mg(2+) export activity of CorC. | |||
Structural basis for the Mg(2+) recognition and regulation of the CorC Mg(2+) transporter.,Huang Y, Jin F, Funato Y, Xu Z, Zhu W, Wang J, Sun M, Zhao Y, Yu Y, Miki H, Hattori M Sci Adv. 2021 Feb 10;7(7). pii: 7/7/eabe6140. doi: 10.1126/sciadv.abe6140. Print , 2021 Feb. PMID:33568487<ref>PMID:33568487</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7cff" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Thermus parvatiensis dwivedi et al. 2015]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hattori M]] | [[Category: Hattori, M]] | ||
[[Category: Huang Y]] | [[Category: Huang, Y]] | ||
[[Category: Jin F]] | [[Category: Jin, F]] | ||
[[Category: Transport protein]] | |||
[[Category: Transporter]] | |||
Revision as of 21:02, 10 March 2021
Structure of the thermostabilized transmembrane domain of the bacterial CNNM/CorC family Mg2+ transporter in complex with Mg2+Structure of the thermostabilized transmembrane domain of the bacterial CNNM/CorC family Mg2+ transporter in complex with Mg2+
Structural highlights
Publication Abstract from PubMedThe CNNM/CorC family proteins are Mg(2+) transporters that are widely distributed in all domains of life. In bacteria, CorC has been implicated in the survival of pathogenic microorganisms. In humans, CNNM proteins are involved in various biological events, such as body absorption/reabsorption of Mg(2+) and genetic disorders. Here, we determined the crystal structure of the Mg(2+)-bound CorC TM domain dimer. Each protomer has a single Mg(2+) binding site with a fully dehydrated Mg(2+) ion. The residues at the Mg(2+) binding site are strictly conserved in both human CNNM2 and CNNM4, and many of these residues are associated with genetic diseases. Furthermore, we determined the structures of the CorC cytoplasmic region containing its regulatory ATP-binding domain. A combination of structural and functional analyses not only revealed the potential interface between the TM and cytoplasmic domains but also showed that ATP binding is important for the Mg(2+) export activity of CorC. Structural basis for the Mg(2+) recognition and regulation of the CorC Mg(2+) transporter.,Huang Y, Jin F, Funato Y, Xu Z, Zhu W, Wang J, Sun M, Zhao Y, Yu Y, Miki H, Hattori M Sci Adv. 2021 Feb 10;7(7). pii: 7/7/eabe6140. doi: 10.1126/sciadv.abe6140. Print , 2021 Feb. PMID:33568487[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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