4dxw

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dxw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alpha_proteobacterium_HIMB114 Alpha proteobacterium HIMB114]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DXW FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dxw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alpha_proteobacterium_HIMB114 Alpha proteobacterium HIMB114]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DXW 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=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PX4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PX4</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]] 3.052&#8491;</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=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PX4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PX4</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=4dxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dxw OCA], [https://pdbe.org/4dxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dxw RCSB], [https://www.ebi.ac.uk/pdbsum/4dxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dxw ProSAT]</span></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=4dxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dxw OCA], [https://pdbe.org/4dxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dxw RCSB], [https://www.ebi.ac.uk/pdbsum/4dxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dxw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/D0RMU8_9PROT D0RMU8_9PROT]]
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[https://www.uniprot.org/uniprot/D0RMU8_9PROT D0RMU8_9PROT]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Voltage-gated sodium (Na(v)) channels are essential for the rapid depolarization of nerve and muscle, and are important drug targets. Determination of the structures of Na(v) channels will shed light on ion channel mechanisms and facilitate potential clinical applications. A family of bacterial Na(v) channels, exemplified by the Na(+)-selective channel of bacteria (NaChBac), provides a useful model system for structure-function analysis. Here we report the crystal structure of Na(v)Rh, a NaChBac orthologue from the marine alphaproteobacterium HIMB114 (Rickettsiales sp. HIMB114; denoted Rh), at 3.05 A resolution. The channel comprises an asymmetric tetramer. The carbonyl oxygen atoms of Thr 178 and Leu 179 constitute an inner site within the selectivity filter where a hydrated Ca(2+) resides in the crystal structure. The outer mouth of the Na(+) selectivity filter, defined by Ser 181 and Glu 183, is closed, as is the activation gate at the intracellular side of the pore. The voltage sensors adopt a depolarized conformation in which all the gating charges are exposed to the extracellular environment. We propose that Na(v)Rh is in an 'inactivated' conformation. Comparison of Na(v)Rh with Na(v)Ab reveals considerable conformational rearrangements that may underlie the electromechanical coupling mechanism of voltage-gated channels.
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Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel.,Zhang X, Ren W, DeCaen P, Yan C, Tao X, Tang L, Wang J, Hasegawa K, Kumasaka T, He J, Wang J, Clapham DE, Yan N Nature. 2012 May 20;486(7401):130-4. doi: 10.1038/nature11054. PMID:22678295<ref>PMID:22678295</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 4dxw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of NavRh, a voltage-gated sodium channel

PDB ID 4dxw

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