5n78: Difference between revisions
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==Crystal structure of the cytosolic domain of the CorA Mg2+ channel from Escherichia coli in complex with magnesium and cobalt hexammine== | |||
<StructureSection load='5n78' size='340' side='right' caption='[[5n78]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n78]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N78 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</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=5n78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n78 OCA], [http://pdbe.org/5n78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n78 RCSB], [http://www.ebi.ac.uk/pdbsum/5n78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n78 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CORA_ECOLI CORA_ECOLI]] Mediates influx of magnesium ions. Can also mediate cobalt and manganese uptake (PubMed:780341). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high (By similarity).[UniProtKB:Q9WZ31]<ref>PMID:780341</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Structures of the Mg2+ bound (closed) and apo (open) states of CorA suggests that channel gating is accomplished by rigid-body motions between symmetric and asymmetric assemblies of the cytosolic portions of the five subunits in response to ligand (Mg2+) binding/unbinding at interfacial sites. Here, we structurally and biochemically characterize the isolated cytosolic domain from Escherichia coli CorA. The data reveal an Mg2+-ligand binding site located in a novel position between each of the five subunits and two Mg2+ ions trapped inside the pore. Soaking experiments show that cobalt hexammine outcompetes Mg2+ at the pore site closest to the membrane. This represents the first structural information of how an analog of hexa-hydrated Mg2+ (and competitive inhibitor of CorA) associates to the CorA pore. Biochemical data on the isolated cytoplasmic domain and full-length protein suggests that gating of the CorA channel is governed cooperatively. | |||
Structure and Cooperativity of the Cytosolic Domain of the CorA Mg2+ Channel from Escherichia coli.,Lerche M, Sandhu H, Flockner L, Hogbom M, Rapp M Structure. 2017 Aug 1;25(8):1175-1186.e4. doi: 10.1016/j.str.2017.05.024. Epub, 2017 Jun 29. PMID:28669631<ref>PMID:28669631</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5n78" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Flockner, L]] | |||
[[Category: Hogbom, M]] | [[Category: Hogbom, M]] | ||
[[Category: Lerche, M]] | [[Category: Lerche, M]] | ||
[[Category: Rapp, M]] | [[Category: Rapp, M]] | ||
[[Category: Sandhu, H]] | |||
[[Category: Homopentamer complex transport membrane]] | |||
[[Category: Transport protein]] | |||
