5aji: Difference between revisions
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=R1A:3-{[(2,2,5,5-TETRAMETHYL-1-OXO-2,5-DIHYDRO-1H-PYRROLIUM-3-YL)METHYL]DISULFANYL}-D-ALANINE'>R1A</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=R1A:3-{[(2,2,5,5-TETRAMETHYL-1-OXO-2,5-DIHYDRO-1H-PYRROLIUM-3-YL)METHYL]DISULFANYL}-D-ALANINE'>R1A</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ait|5ait]], [[5aiu|5aiu]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ait|5ait]], [[5aiu|5aiu]]</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=5aji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aji OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5aji RCSB], [http://www.ebi.ac.uk/pdbsum/5aji PDBsum]</span></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=5aji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aji OCA], [http://pdbe.org/5aji PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aji RCSB], [http://www.ebi.ac.uk/pdbsum/5aji PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MSCS_ECO57 MSCS_ECO57]] Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage (By similarity). | [[http://www.uniprot.org/uniprot/MSCS_ECO57 MSCS_ECO57]] Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage (By similarity). | ||
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== Publication Abstract from PubMed == | |||
The ability of proteins to sense membrane tension is pervasive in biology. A higher-resolution structure of the Escherichia coli small-conductance mechanosensitive channel MscS identifies alkyl chains inside pockets formed by the transmembrane helices (TMs). Purified MscS contains E. coli lipids, and fluorescence quenching demonstrates that phospholipid acyl chains exchange between bilayer and TM pockets. Molecular dynamics and biophysical analyses show that the volume of the pockets and thus the number of lipid acyl chains within them decreases upon channel opening. Phospholipids with one acyl chain per head group (lysolipids) displace normal phospholipids (with two acyl chains) from MscS pockets and trigger channel opening. We propose that the extent of acyl-chain interdigitation in these pockets determines the conformation of MscS. When interdigitation is perturbed by increased membrane tension or by lysolipids, the closed state becomes unstable, and the channel gates. | |||
The role of lipids in mechanosensation.,Pliotas C, Dahl AC, Rasmussen T, Mahendran KR, Smith TK, Marius P, Gault J, Banda T, Rasmussen A, Miller S, Robinson CV, Bayley H, Sansom MS, Booth IR, Naismith JH Nat Struct Mol Biol. 2015 Nov 9. doi: 10.1038/nsmb.3120. PMID:26551077<ref>PMID:26551077</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5aji" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||