3rw0: Difference between revisions
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<StructureSection load='3rw0' size='340' side='right'caption='[[3rw0]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='3rw0' size='340' side='right'caption='[[3rw0]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rw0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3rw0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliarcobacter_butzleri_RM4018 Aliarcobacter butzleri RM4018]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RW0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3rw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rw0 OCA], [https://pdbe.org/3rw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3rw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rw0 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=3rw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rw0 OCA], [https://pdbe.org/3rw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3rw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rw0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A8EVM5_ALIB4 A8EVM5_ALIB4] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aliarcobacter butzleri RM4018]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Catterall | [[Category: Catterall WA]] | ||
[[Category: Payandeh | [[Category: Payandeh J]] | ||
[[Category: Scheuer | [[Category: Scheuer T]] | ||
[[Category: Zheng | [[Category: Zheng N]] | ||
Latest revision as of 13:24, 6 November 2024
Structural highlights
FunctionPublication Abstract from PubMedVoltage-gated sodium (Na(V)) channels initiate electrical signalling in excitable cells and are the molecular targets for drugs and disease mutations, but the structural basis for their voltage-dependent activation, ion selectivity and drug block is unknown. Here we report the crystal structure of a voltage-gated Na(+) channel from Arcobacter butzleri (NavAb) captured in a closed-pore conformation with four activated voltage sensors at 2.7 A resolution. The arginine gating charges make multiple hydrophilic interactions within the voltage sensor, including unanticipated hydrogen bonds to the protein backbone. Comparisons to previous open-pore potassium channel structures indicate that the voltage-sensor domains and the S4-S5 linkers dilate the central pore by pivoting together around a hinge at the base of the pore module. The NavAb selectivity filter is short, approximately 4.6 A wide, and water filled, with four acidic side chains surrounding the narrowest part of the ion conduction pathway. This unique structure presents a high-field-strength anionic coordination site, which confers Na(+) selectivity through partial dehydration via direct interaction with glutamate side chains. Fenestrations in the sides of the pore module are unexpectedly penetrated by fatty acyl chains that extend into the central cavity, and these portals are large enough for the entry of small, hydrophobic pore-blocking drugs. This structure provides the template for understanding electrical signalling in excitable cells and the actions of drugs used for pain, epilepsy and cardiac arrhythmia at the atomic level. The crystal structure of a voltage-gated sodium channel.,Payandeh J, Scheuer T, Zheng N, Catterall WA Nature. 2011 Jul 10;475(7356):353-8. doi: 10.1038/nature10238. PMID:21743477[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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