9yyd: Difference between revisions

Line 1:

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

The entry ~~9yyd~~ is ~~ON HOLD until Paper Publication~~

==the structure of ERMA Mg2+ bound form==

== Structural highlights ==

<table><tr><td colspan='2'>[[9yyd]] is a 1 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=9YYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YYD FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEV:(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PEV</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=9yyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9yyd OCA], [https://pdbe.org/9yyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9yyd RCSB], [https://www.ebi.ac.uk/pdbsum/9yyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9yyd ProSAT]</span></td></tr>

</table>

== Disease ==

[https://www.uniprot.org/uniprot/TMM94_HUMAN TMM94_HUMAN] TMEM94-associated congenital heart defect-facial dysmorphism-developmental delay syndrome. The disease is caused by variants affecting the gene represented in this entry.

== Function ==

[https://www.uniprot.org/uniprot/TMM94_HUMAN TMM94_HUMAN] Could function in the uptake of Mg(2+) from the cytosol into the endoplasmic reticulum and regulate intracellular Mg(2+) homeostasis.<ref>PMID:38513662</ref>

== Publication Abstract from PubMed ==

Magnesium (Mg(2+)) is the most abundant divalent cation in cells, yet the mechanisms mediating its organellar transport remain poorly defined. We identify endoplasmic reticulum (ER) Mg(2+) adenosine triphosphatase (ATPase) (ERMA) as the transporter that drives Mg(2+) uptake into the ER lumen, establishing the ER as a bi-ionic intracellular reservoir. MagFRET biosensors targeted to the ER demonstrate that ERMA mediates dynamic ER Mg(2+) storage and robust adenosine 5'-triphosphate-dependent Mg(2+) uptake reaching 15 to 30 millimolar. Cryo-electron microscopy structures of human and mouse ERMA reveal a P-type ATPase fold with an unwound transmembrane 4 (TM4) that coordinates Mg(2+) via the unique PILP backbone and the TM5 residue Q1110, whose mutation markedly impairs ERMA-mediated Mg(2+) uptake. Functional reconstitution of domain mutants, ERMA-SERCA chimeras, and pathogenic variants confirm ERMA as an ER-resident Mg(2+) pump and gatekeeper of ER Mg(2+) ionic equilibrium.

~~Authors:~~ Shi, N., Jiang, Y.

Structural and mutational insights define ERMA as the ER Mg(2+) ATPase and reservoir gatekeeper.,Venkatesan M, Oldham ML, Shi N, Chidambaram A, Vishnu N, Madesh AK, Bentz K, Stathopulos PB, Kalathur RC, Jiang Y, Madesh M Sci Adv. 2026 Jul 3;12(27):eaef4971. doi: 10.1126/sciadv.aef4971. Epub 2026 Jul , 1. PMID:42384784<ref>PMID:42384784</ref>

~~Description:~~ the ~~structure~~ of ~~ERMA Mg2+ bound form~~

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

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

</div>

[[Category: Jiang, Y]]

[[Category: Shi, N]]

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Jiang Y]]

[[Category: Shi N]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9yyd is ON HOLD  until Paper Publication
+==the structure of ERMA Mg2+ bound form==
+<StructureSection load='9yyd' size='340' side='right'caption='[[9yyd]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9yyd]] is a 1 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=9YYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YYD FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEV:(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PEV</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=9yyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9yyd OCA], [https://pdbe.org/9yyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9yyd RCSB], [https://www.ebi.ac.uk/pdbsum/9yyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9yyd ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/TMM94_HUMAN TMM94_HUMAN] TMEM94-associated congenital heart defect-facial dysmorphism-developmental delay syndrome. The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/TMM94_HUMAN TMM94_HUMAN] Could function in the uptake of Mg(2+) from the cytosol into the endoplasmic reticulum and regulate intracellular Mg(2+) homeostasis.<ref>PMID:38513662</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Magnesium (Mg(2+)) is the most abundant divalent cation in cells, yet the mechanisms mediating its organellar transport remain poorly defined. We identify endoplasmic reticulum (ER) Mg(2+) adenosine triphosphatase (ATPase) (ERMA) as the transporter that drives Mg(2+) uptake into the ER lumen, establishing the ER as a bi-ionic intracellular reservoir. MagFRET biosensors targeted to the ER demonstrate that ERMA mediates dynamic ER Mg(2+) storage and robust adenosine 5'-triphosphate-dependent Mg(2+) uptake reaching 15 to 30 millimolar. Cryo-electron microscopy structures of human and mouse ERMA reveal a P-type ATPase fold with an unwound transmembrane 4 (TM4) that coordinates Mg(2+) via the unique PILP backbone and the TM5 residue Q1110, whose mutation markedly impairs ERMA-mediated Mg(2+) uptake. Functional reconstitution of domain mutants, ERMA-SERCA chimeras, and pathogenic variants confirm ERMA as an ER-resident Mg(2+) pump and gatekeeper of ER Mg(2+) ionic equilibrium.
-Authors: Shi, N., Jiang, Y.
+Structural and mutational insights define ERMA as the ER Mg(2+) ATPase and reservoir gatekeeper.,Venkatesan M, Oldham ML, Shi N, Chidambaram A, Vishnu N, Madesh AK, Bentz K, Stathopulos PB, Kalathur RC, Jiang Y, Madesh M Sci Adv. 2026 Jul 3;12(27):eaef4971. doi: 10.1126/sciadv.aef4971. Epub 2026 Jul , 1. PMID:42384784<ref>PMID:42384784</ref>
-Description: the structure of ERMA Mg2+ bound form
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Jiang, Y]]
+<div class="pdbe-citations 9yyd" style="background-color:#fffaf0;"></div>
-[[Category: Shi, N]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Jiang Y]]
+[[Category: Shi N]]