6n7e: Difference between revisions

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~~'''Unreleased structure'''~~

The entry ~~6n7e~~ is ~~ON HOLD until Paper Publication~~

==Crystal structure of the cytosolic domain of human CNNM2 in complex with AMP-PNP and Mg2+==

== Structural highlights ==

<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='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='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='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>

</table>

== Disease ==

[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 ==

[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).

== 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.

~~Authors~~:

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<ref>PMID:31864811</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Chen YS]]

[[Category: Gehring K]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6n7e is ON HOLD  until Paper Publication
+==Crystal structure of the cytosolic domain of human CNNM2 in complex with AMP-PNP and Mg2+==
+<StructureSection load='6n7e' size='340' side='right'caption='[[6n7e]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</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='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>
+</table>
+== Disease ==
+[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 ==
+[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;">
+== 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.
-Authors:
+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<ref>PMID:31864811</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6n7e" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Chen YS]]
+[[Category: Gehring K]]