4wib: Difference between revisions
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''' | ==Crystal structure of Magnesium transporter MgtE== | ||
<StructureSection load='4wib' size='340' side='right' caption='[[4wib]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4wib]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WIB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4wib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wib OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wib RCSB], [http://www.ebi.ac.uk/pdbsum/4wib PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Magnesium is the most abundant divalent cation in living cells and is crucial to several biological processes. MgtE is a Mg(2+) channel distributed in all domains of life that contributes to the maintenance of cellular Mg(2+) homeostasis. Here we report the high-resolution crystal structures of the transmembrane domain of MgtE, bound to Mg(2+), Mn(2+) and Ca(2+). The high-resolution Mg(2+)-bound crystal structure clearly visualized the hydrated Mg(2+) ion within its selectivity filter. Based on those structures and biochemical analyses, we propose a cation selectivity mechanism for MgtE in which the geometry of the hydration shell of the fully hydrated Mg(2+) ion is recognized by the side-chain carboxylate groups in the selectivity filter. This is in contrast to the K(+)-selective filter of KcsA, which recognizes a dehydrated K(+) ion. Our results further revealed a cation-binding site on the periplasmic side, which regulate channel opening and prevents conduction of near-cognate cations. | |||
Structural basis for ion selectivity revealed by high-resolution crystal structure of Mg(2+) channel MgtE.,Takeda H, Hattori M, Nishizawa T, Yamashita K, Shah ST, Caffrey M, Maturana AD, Ishitani R, Nureki O Nat Commun. 2014 Nov 4;5:5374. doi: 10.1038/ncomms6374. PMID:25367295<ref>PMID:25367295</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caffrey, M]] | |||
[[Category: Hattori, M]] | |||
[[Category: Ishitani, R]] | |||
[[Category: Maturana, A D]] | |||
[[Category: Nishizawa, T]] | |||
[[Category: Nureki, O]] | |||
[[Category: Shah, S T.A]] | |||
[[Category: Takeda, H]] | |||
[[Category: Yamashita, K]] | |||
[[Category: Channel]] | |||
[[Category: Magnesium]] | |||
[[Category: Transporter]] | |||