6pvr

<StructureSection load='6pvr' size='340' side='right'caption='[[6pvr]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[6pvr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_b_virus_(b/maryland/1/01) Influenza b virus (b/maryland/1/01)]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PVR FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1601064 Influenza B virus (B/Maryland/1/01)])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pvr OCA], [http://pdbe.org/6pvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pvr RCSB], [http://www.ebi.ac.uk/pdbsum/6pvr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pvr ProSAT]</span></td></tr>

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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.

 

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== References ==

[[Category: Hong, M]]

[[Category: Loftis, A R]]

[[Category: Mandala, V S]]

[[Category: Pentelute, B L]]

[[Category: Shcherbakov, A S]]

[[Category: Viral protein]]