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6pvr
From Proteopedia
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==Influenza B M2 Proton Channel in the Closed State - SSNMR Structure at pH 7.5== | ==Influenza B M2 Proton Channel in the Closed State - SSNMR Structure at pH 7.5== | ||
| - | <StructureSection load='6pvr' size='340' side='right'caption='[[6pvr | + | <StructureSection load='6pvr' size='340' side='right'caption='[[6pvr]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6pvr]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6pvr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_B_virus_(B/Maryland/1/2001) Influenza B virus (B/Maryland/1/2001)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PVR 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">Solid-state NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pvr OCA], [https://pdbe.org/6pvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pvr RCSB], [https://www.ebi.ac.uk/pdbsum/6pvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pvr ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The influenza B M2 (BM2) proton channel is activated by acidic pH to mediate virus uncoating. Unlike influenza A M2 (AM2), which conducts protons with strong inward rectification, BM2 conducts protons both inward and outward. Here we report 1.4- and 1.5-A solid-state NMR structures of the transmembrane domain of the closed and open BM2 channels in a phospholipid environment. Upon activation, the transmembrane helices increase the tilt angle by 6 degrees and the average pore diameter enlarges by 2.1 A. BM2 thus undergoes a scissor motion for activation, which differs from the alternating-access motion of AM2. These results indicate that asymmetric proton conduction requires a backbone hinge motion, whereas bidirectional conduction is achieved by a symmetric scissor motion. The proton-selective histidine and gating tryptophan in the open BM2 reorient on the microsecond timescale, similar to AM2, indicating that side chain dynamics are the essential driver of proton shuttling. | ||
| - | + | ==See Also== | |
| - | + | *[[Ion channels 3D structures|Ion channels 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hong | + | [[Category: Hong M]] |
| - | [[Category: Loftis | + | [[Category: Loftis AR]] |
| - | [[Category: Mandala | + | [[Category: Mandala VS]] |
| - | [[Category: Pentelute | + | [[Category: Pentelute BL]] |
| - | [[Category: Shcherbakov | + | [[Category: Shcherbakov AS]] |
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Current revision
Influenza B M2 Proton Channel in the Closed State - SSNMR Structure at pH 7.5
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