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5x9h

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Current revision (10:17, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5x9h' size='340' side='right'caption='[[5x9h]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='5x9h' size='340' side='right'caption='[[5x9h]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5x9h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X9H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5x9h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X9H FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.598&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x9g|5x9g]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9h OCA], [http://pdbe.org/5x9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9h RCSB], [http://www.ebi.ac.uk/pdbsum/5x9h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9h ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5x9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9h OCA], [https://pdbe.org/5x9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x9h RCSB], [https://www.ebi.ac.uk/pdbsum/5x9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MGTE_THET8 MGTE_THET8]] Acts as a highly selective magnesium channel.<ref>PMID:17700703</ref> <ref>PMID:19798051</ref>
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[https://www.uniprot.org/uniprot/MGTE_THET8 MGTE_THET8] Acts as a highly selective magnesium channel.<ref>PMID:17700703</ref> <ref>PMID:19798051</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Magnesium is an essential ion for numerous physiological processes. MgtE is a Mg2+ selective channel involved in the maintenance of intracellular Mg2+ homeostasis, whose gating is regulated by intracellular Mg2+ levels. Here, we report that ATP binds to MgtE, regulating its Mg2+-dependent gating. Crystal structures of MgtE-ATP complex show that ATP binds to the intracellular CBS domain of MgtE. Functional studies support that ATP binding to MgtE enhances the intracellular domain affinity for Mg2+ within physiological concentrations of this divalent cation, enabling MgtE to function as an in vivo Mg2+ sensor. ATP dissociation from MgtE upregulates Mg2+ influx at both high and low intracellular Mg2+ concentrations. Using site-directed mutagenesis and structure based-electrophysiological and biochemical analyses, we identify key residues and main structural changes involved in the process. This work provides the molecular basis of ATP-dependent modulation of MgtE in Mg2+ homeostasis.MgtE is an Mg2+ transporter involved in Mg2+ homeostasis. Here, the authors report that ATP regulates the Mg+2-dependent gating of MgtE and use X-ray crystallography combined with functional studies to propose the molecular mechanisms involved in this process.
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ATP-dependent modulation of MgtE in Mg2+ homeostasis.,Tomita A, Zhang M, Jin F, Zhuang W, Takeda H, Maruyama T, Osawa M, Hashimoto KI, Kawasaki H, Ito K, Dohmae N, Ishitani R, Shimada I, Yan Z, Hattori M, Nureki O Nat Commun. 2017 Jul 27;8(1):148. doi: 10.1038/s41467-017-00082-w. PMID:28747715<ref>PMID:28747715</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5x9h" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hattori, M]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Nureki, O]]
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[[Category: Hattori M]]
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[[Category: Tomita, A]]
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[[Category: Nureki O]]
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[[Category: Channel]]
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[[Category: Tomita A]]
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[[Category: Metal transport]]
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Current revision

Crystal structure of the Mg2+ channel MgtE in complex with ATP

PDB ID 5x9h

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