6pvt
From Proteopedia
(Difference between revisions)
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<StructureSection load='6pvt' size='340' side='right'caption='[[6pvt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='6pvt' size='340' side='right'caption='[[6pvt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6pvt]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PVT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6pvt]] 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=6PVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pvt OCA], [http://pdbe.org/6pvt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pvt RCSB], [http://www.ebi.ac.uk/pdbsum/6pvt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pvt ProSAT]</span></td></tr> | + | </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=6pvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pvt OCA], [http://pdbe.org/6pvt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pvt RCSB], [http://www.ebi.ac.uk/pdbsum/6pvt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pvt 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. | ||
+ | |||
+ | 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> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6pvt" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 07:28, 19 February 2020
Influenza B M2 Proton Channel in the Open State - SSNMR Structure at pH 4.5
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