6pvt: Difference between revisions
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==Influenza B M2 Proton Channel in the Open State - SSNMR Structure at pH 4.5== | |||
<StructureSection load='6pvt' size='340' side='right'caption='[[6pvt]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6pvt]] 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=6PVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PVT 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=6pvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pvt OCA], [https://pdbe.org/6pvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pvt RCSB], [https://www.ebi.ac.uk/pdbsum/6pvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pvt ProSAT]</span></td></tr> | |||
</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. | |||
Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism.,Mandala VS, Loftis AR, Shcherbakov AA, Pentelute BL, Hong M Nat Struct Mol Biol. 2020 Feb;27(2):160-167. doi: 10.1038/s41594-019-0371-2. Epub, 2020 Feb 3. PMID:32015551<ref>PMID:32015551</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6pvt" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Hong M]] | |||
[[Category: Loftis AR]] | |||
[[Category: Mandala VS]] | |||
[[Category: Pentelute BL]] | |||
[[Category: Shcherbakov AS]] | |||
Latest revision as of 10:59, 14 June 2023
Influenza B M2 Proton Channel in the Open State - SSNMR Structure at pH 4.5
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