7pg8: Difference between revisions
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==== | ==NaV_Ae1/Sp1CTD_pore-ANT05 complex== | ||
<StructureSection load='7pg8' size='340' side='right'caption='[[7pg8]]' scene=''> | <StructureSection load='7pg8' size='340' side='right'caption='[[7pg8]], [[Resolution|resolution]] 4.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pg8]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalilimnicola_ehrlichii_MLHE-1 Alkalilimnicola ehrlichii MLHE-1], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Ruegeria_pomeroyi_DSS-3 Ruegeria pomeroyi DSS-3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PG8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PG8 FirstGlance]. <br> | ||
</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=7pg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pg8 OCA], [https://pdbe.org/7pg8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pg8 RCSB], [https://www.ebi.ac.uk/pdbsum/7pg8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pg8 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.5Å</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=7pg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pg8 OCA], [https://pdbe.org/7pg8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pg8 RCSB], [https://www.ebi.ac.uk/pdbsum/7pg8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pg8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0ABW0_ALKEH Q0ABW0_ALKEH] [https://www.uniprot.org/uniprot/F7IVA8_RUEPO F7IVA8_RUEPO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Every voltage-gated ion channel (VGIC) has a pore domain (PD) made from four subunits, each comprising an antiparallel transmembrane helix pair bridged by a loop. The extent to which PD subunit structure requires quaternary interactions is unclear. Here, we present crystal structures of a set of bacterial voltage-gated sodium channel (BacNaV) 'pore only' proteins that reveal a surprising collection of non-canonical quaternary arrangements in which the PD tertiary structure is maintained. This context-independent structural robustness, supported by molecular dynamics simulations, indicates that VGIC-PD tertiary structure is independent of quaternary interactions. This fold occurs throughout the VGIC superfamily and in diverse transmembrane and soluble proteins. Strikingly, characterization of PD subunit-binding Fabs indicates that non-canonical quaternary PD conformations can occur in full-length VGICs. Together, our data demonstrate that the VGIC-PD is an autonomously folded unit. This property has implications for VGIC biogenesis, understanding functional states, de novo channel design, and VGIC structural origins. | |||
Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.,Arrigoni C, Lolicato M, Shaya D, Rohaim A, Findeisen F, Fong LK, Colleran CM, Dominik P, Kim SS, Schuermann JP, DeGrado WF, Grabe M, Kossiakoff AA, Minor DL Jr Nat Struct Mol Biol. 2022 Jun 2. pii: 10.1038/s41594-022-00775-x. doi:, 10.1038/s41594-022-00775-x. PMID:35655098<ref>PMID:35655098</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7pg8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Alkalilimnicola ehrlichii MLHE-1]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ruegeria pomeroyi DSS-3]] | ||
[[Category: Arrigoni C]] | |||
[[Category: Lolicato M]] | |||
Latest revision as of 16:05, 1 February 2024
NaV_Ae1/Sp1CTD_pore-ANT05 complexNaV_Ae1/Sp1CTD_pore-ANT05 complex
Structural highlights
FunctionPublication Abstract from PubMedEvery voltage-gated ion channel (VGIC) has a pore domain (PD) made from four subunits, each comprising an antiparallel transmembrane helix pair bridged by a loop. The extent to which PD subunit structure requires quaternary interactions is unclear. Here, we present crystal structures of a set of bacterial voltage-gated sodium channel (BacNaV) 'pore only' proteins that reveal a surprising collection of non-canonical quaternary arrangements in which the PD tertiary structure is maintained. This context-independent structural robustness, supported by molecular dynamics simulations, indicates that VGIC-PD tertiary structure is independent of quaternary interactions. This fold occurs throughout the VGIC superfamily and in diverse transmembrane and soluble proteins. Strikingly, characterization of PD subunit-binding Fabs indicates that non-canonical quaternary PD conformations can occur in full-length VGICs. Together, our data demonstrate that the VGIC-PD is an autonomously folded unit. This property has implications for VGIC biogenesis, understanding functional states, de novo channel design, and VGIC structural origins. Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.,Arrigoni C, Lolicato M, Shaya D, Rohaim A, Findeisen F, Fong LK, Colleran CM, Dominik P, Kim SS, Schuermann JP, DeGrado WF, Grabe M, Kossiakoff AA, Minor DL Jr Nat Struct Mol Biol. 2022 Jun 2. pii: 10.1038/s41594-022-00775-x. doi:, 10.1038/s41594-022-00775-x. PMID:35655098[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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