6mjh: Difference between revisions
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The entry | ==The S31N mutant of the influenza A M2 proton channel in two distinct conformational states== | ||
<StructureSection load='6mjh' size='340' side='right'caption='[[6mjh]], [[Resolution|resolution]] 2.06Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mjh]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MJH FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=6mjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mjh OCA], [http://pdbe.org/6mjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mjh RCSB], [http://www.ebi.ac.uk/pdbsum/6mjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mjh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A0R5TVW3_9INFA A0A0R5TVW3_9INFA]] Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry.[RuleBase:RU361247] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The amantadine-resistant S31N mutant of the influenza A M2 proton channel has become prevalent in currently circulating viruses. Here we have solved an X-ray crystal structure of M2(22-46) S31N that contains two distinct conformational states within its asymmetric unit. This structure reveals the mechanism of adamantane resistance in both conformational states of the M2 channel. In the Inward(open) conformation, the mutant Asn31 side chain faces the channel pore and sterically blocks the adamantane binding site. In the Inward(closed) conformation, Asn31 forms hydrogen bonds with carbonyls at the monomer-monomer interface, which twists the monomer helices and constricts the channel pore at the drug binding site. We also examine M2(19-49) WT and S31N using solution NMR spectroscopy, and show that distribution of the two conformational states is dependent on both detergent choice and experimental pH. | |||
X-ray crystal structure of the influenza A M2 proton channel S31N mutant in two conformational states: an open and shut case.,Thomaston JL, Wu Y, Polizzi N, Liu L, Wang J, DeGrado WF J Am Chem Soc. 2019 Jun 11. doi: 10.1021/jacs.9b02196. PMID:31184871<ref>PMID:31184871</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6mjh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: DeGrado, W F]] | |||
[[Category: Thomaston, J L]] | |||
[[Category: Membrane protein]] | |||
[[Category: Proton channel]] | |||
[[Category: S31n]] | |||
[[Category: Viral protein]] | |||
Revision as of 09:54, 26 June 2019
The S31N mutant of the influenza A M2 proton channel in two distinct conformational statesThe S31N mutant of the influenza A M2 proton channel in two distinct conformational states
Structural highlights
Function[A0A0R5TVW3_9INFA] Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry.[RuleBase:RU361247] Publication Abstract from PubMedThe amantadine-resistant S31N mutant of the influenza A M2 proton channel has become prevalent in currently circulating viruses. Here we have solved an X-ray crystal structure of M2(22-46) S31N that contains two distinct conformational states within its asymmetric unit. This structure reveals the mechanism of adamantane resistance in both conformational states of the M2 channel. In the Inward(open) conformation, the mutant Asn31 side chain faces the channel pore and sterically blocks the adamantane binding site. In the Inward(closed) conformation, Asn31 forms hydrogen bonds with carbonyls at the monomer-monomer interface, which twists the monomer helices and constricts the channel pore at the drug binding site. We also examine M2(19-49) WT and S31N using solution NMR spectroscopy, and show that distribution of the two conformational states is dependent on both detergent choice and experimental pH. X-ray crystal structure of the influenza A M2 proton channel S31N mutant in two conformational states: an open and shut case.,Thomaston JL, Wu Y, Polizzi N, Liu L, Wang J, DeGrado WF J Am Chem Soc. 2019 Jun 11. doi: 10.1021/jacs.9b02196. PMID:31184871[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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