7pgg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NaVAb1p detergent (DM)== | |
| + | <StructureSection load='7pgg' size='340' side='right'caption='[[7pgg]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7pgg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcanivorax_borkumensis Alcanivorax borkumensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PGG 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]] 2.85Å</td></tr> | ||
| + | <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=VVA:2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}ETHYL+HEPTADECANOATE'>VVA</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=7pgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pgg OCA], [https://pdbe.org/7pgg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pgg RCSB], [https://www.ebi.ac.uk/pdbsum/7pgg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pgg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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 (BacNa(V)) '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;29(6):537-548. doi: 10.1038/s41594-022-00775-x. , Epub 2022 Jun 2. PMID:35655098<ref>PMID:35655098</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7pgg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Alcanivorax borkumensis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrigoni C]] | ||
| + | [[Category: Lolicato M]] | ||
Current revision
NaVAb1p detergent (DM)
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