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| | <StructureSection load='6n7e' size='340' side='right'caption='[[6n7e]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='6n7e' size='340' side='right'caption='[[6n7e]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6n7e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N7E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6n7e]] is a 4 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=6N7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N7E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mn6|6mn6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CNNM2, ACDP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6n7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n7e OCA], [https://pdbe.org/6n7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n7e RCSB], [https://www.ebi.ac.uk/pdbsum/6n7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n7e ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6n7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n7e OCA], [http://pdbe.org/6n7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n7e RCSB], [http://www.ebi.ac.uk/pdbsum/6n7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n7e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/CNNM2_HUMAN CNNM2_HUMAN]] Familial primary hypomagnesemia with normocalcuria and normocalcemia. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/CNNM2_HUMAN CNNM2_HUMAN] Familial primary hypomagnesemia with normocalcuria and normocalcemia. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CNNM2_HUMAN CNNM2_HUMAN]] Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+) (By similarity). | + | [https://www.uniprot.org/uniprot/CNNM2_HUMAN CNNM2_HUMAN] Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+) (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, Y S]] | + | [[Category: Chen YS]] |
| - | [[Category: Gehring, K]] | + | [[Category: Gehring K]] |
| - | [[Category: Atp-bound]]
| + | |
| - | [[Category: Closed conformation]]
| + | |
| - | [[Category: Cnnm2]]
| + | |
| - | [[Category: Cyclic nucleotide-binding homology domain]]
| + | |
| - | [[Category: Cystathionine-beta-synthase domain]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Mg2+ transporter]]
| + | |
| Structural highlights
Disease
CNNM2_HUMAN Familial primary hypomagnesemia with normocalcuria and normocalcemia. The disease is caused by mutations affecting the gene represented in this entry.
Function
CNNM2_HUMAN Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+) (By similarity).
Publication Abstract from PubMed
The family of cystathionine-beta-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) is composed of four integral membrane proteins associated with Mg(2+) transport. Structurally, CNNMs contain large cytosolic regions composed of a CBS-pair and a cyclic nucleotide-binding homology (CNBH) domain. How these regulate Mg(2+) transport activity is unknown. Here, we determined the crystal structures of cytosolic fragments in two conformations: Mg(2+)-ATP-analog bound and ligand free. The structures reveal open and closed conformations with functionally important contacts not observed in structures of the individual domains. We also identified a second Mg(2+)-binding region in the CBS-pair domain and a different dimerization interface for the CNBH domain. Analytical ultracentrifugation and isothermal titration calorimetry experiments revealed a tight correlation between Mg(2+)-ATP binding and protein dimerization. Mutations that blocked either function prevented cellular Mg(2+) efflux activity. The results suggest Mg(2+) efflux is regulated by conformational changes associated with Mg(2+)-ATP binding to CNNM CBS-pair domains.
Mg(2+)-ATP Sensing in CNNM, a Putative Magnesium Transporter.,Chen YS, Kozlov G, Fakih R, Yang M, Zhang Z, Kovrigin EL, Gehring K Structure. 2019 Dec 10. pii: S0969-2126(19)30434-4. doi:, 10.1016/j.str.2019.11.016. PMID:31864811[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen YS, Kozlov G, Fakih R, Yang M, Zhang Z, Kovrigin EL, Gehring K. Mg(2+)-ATP Sensing in CNNM, a Putative Magnesium Transporter. Structure. 2019 Dec 10. pii: S0969-2126(19)30434-4. doi:, 10.1016/j.str.2019.11.016. PMID:31864811 doi:http://dx.doi.org/10.1016/j.str.2019.11.016
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