4ltp: Difference between revisions
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== | ==Bacterial sodium channel in high calcium, I222 space group, crystal 2== | ||
[[4ltp]] is a 4 chain structure with sequence from [ | <StructureSection load='4ltp' size='340' side='right'caption='[[4ltp]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ltp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalilimnicola_ehrlichii Alkalilimnicola ehrlichii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LTP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4ltp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ltp OCA], [https://pdbe.org/4ltp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ltp RCSB], [https://www.ebi.ac.uk/pdbsum/4ltp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ltp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0ABW0_ALKEH Q0ABW0_ALKEH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Voltage-gated sodium channels (NaVs) are central elements of cellular excitation. Notwithstanding advances from recent bacterial NaV (BacNaV) structures, key questions about gating and ion selectivity remain. Here, we present a closed conformation of NaVAe1p, a pore-only BacNaV derived from NaVAe1, a BacNaV from the arsenite oxidizer Alkalilimnicola ehrlichei found in Mono Lake, California, that provides insight into both fundamental properties. The structure reveals a pore domain in which the pore-lining S6 helix connects to a helical cytoplasmic tail. Electrophysiological studies of full-length BacNaVs show that two elements defined by the NaVAe1p structure, an S6 activation gate position and the cytoplasmic tail "neck", are central to BacNaV gating. The structure also reveals the selectivity filter ion entry site, termed the "outer ion" site. Comparison with mammalian voltage-gated calcium channel (CaV) selectivity filters, together with functional studies, shows that this site forms a previously unknown determinant of CaV high-affinity calcium binding. Our findings underscore commonalities between BacNaVs and eukaryotic voltage-gated channels and provide a framework for understanding gating and ion permeation in this superfamily. | |||
Structure of a Prokaryotic Sodium Channel Pore Reveals Essential Gating Elements and an Outer Ion Binding Site Common to Eukaryotic Channels.,Shaya D, Findeisen F, Abderemane-Ali F, Arrigoni C, Wong S, Nurva SR, Loussouarn G, Minor DL Jr J Mol Biol. 2013 Oct 10. pii: S0022-2836(13)00636-0. doi:, 10.1016/j.jmb.2013.10.010. PMID:24120938<ref>PMID:24120938</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ltp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alkalilimnicola ehrlichii]] | [[Category: Alkalilimnicola ehrlichii]] | ||
[[Category: Abderemane-Ali | [[Category: Large Structures]] | ||
[[Category: Arrigoni | [[Category: Abderemane-Ali F]] | ||
[[Category: Findeisen | [[Category: Arrigoni C]] | ||
[[Category: Loussouarn | [[Category: Findeisen F]] | ||
[[Category: Minor | [[Category: Loussouarn G]] | ||
[[Category: Nurva | [[Category: Minor DL]] | ||
[[Category: Shaya | [[Category: Reddy Nurva S]] | ||
[[Category: Wong | [[Category: Shaya D]] | ||
[[Category: Wong S]] | |||
Latest revision as of 19:25, 20 September 2023
Bacterial sodium channel in high calcium, I222 space group, crystal 2Bacterial sodium channel in high calcium, I222 space group, crystal 2
Structural highlights
FunctionPublication Abstract from PubMedVoltage-gated sodium channels (NaVs) are central elements of cellular excitation. Notwithstanding advances from recent bacterial NaV (BacNaV) structures, key questions about gating and ion selectivity remain. Here, we present a closed conformation of NaVAe1p, a pore-only BacNaV derived from NaVAe1, a BacNaV from the arsenite oxidizer Alkalilimnicola ehrlichei found in Mono Lake, California, that provides insight into both fundamental properties. The structure reveals a pore domain in which the pore-lining S6 helix connects to a helical cytoplasmic tail. Electrophysiological studies of full-length BacNaVs show that two elements defined by the NaVAe1p structure, an S6 activation gate position and the cytoplasmic tail "neck", are central to BacNaV gating. The structure also reveals the selectivity filter ion entry site, termed the "outer ion" site. Comparison with mammalian voltage-gated calcium channel (CaV) selectivity filters, together with functional studies, shows that this site forms a previously unknown determinant of CaV high-affinity calcium binding. Our findings underscore commonalities between BacNaVs and eukaryotic voltage-gated channels and provide a framework for understanding gating and ion permeation in this superfamily. Structure of a Prokaryotic Sodium Channel Pore Reveals Essential Gating Elements and an Outer Ion Binding Site Common to Eukaryotic Channels.,Shaya D, Findeisen F, Abderemane-Ali F, Arrigoni C, Wong S, Nurva SR, Loussouarn G, Minor DL Jr J Mol Biol. 2013 Oct 10. pii: S0022-2836(13)00636-0. doi:, 10.1016/j.jmb.2013.10.010. PMID:24120938[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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