View source for 6pvt


==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>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Ion channels 3D structures|Ion channels 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Hong M]]
[[Category: Loftis AR]]
[[Category: Mandala VS]]
[[Category: Pentelute BL]]
[[Category: Shcherbakov AS]]