2oar

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Current revision (00:16, 28 December 2023) (edit) (undo)
 
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<StructureSection load='2oar' size='340' side='right'caption='[[2oar]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='2oar' size='340' side='right'caption='[[2oar]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2oar]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycta Mycta]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1msl 1msl]. The November 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Mechanosensitive Channels'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_11 10.2210/rcsb_pdb/mom_2008_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OAR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2oar]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Ra Mycobacterium tuberculosis H37Ra]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1msl 1msl]. The November 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Mechanosensitive Channels'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_11 10.2210/rcsb_pdb/mom_2008_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OAR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mscL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=419947 MYCTA])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></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=2oar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oar OCA], [https://pdbe.org/2oar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oar RCSB], [https://www.ebi.ac.uk/pdbsum/2oar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oar ProSAT]</span></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=2oar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oar OCA], [https://pdbe.org/2oar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oar RCSB], [https://www.ebi.ac.uk/pdbsum/2oar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oar ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MSCL_MYCTU MSCL_MYCTU]] Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell (By similarity).
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[https://www.uniprot.org/uniprot/MSCL_MYCTA MSCL_MYCTA] Channel that opens in response to stretch forces in the membrane lipid bilayer. The force required to trigger channel opening depends on the nature of the membrane lipids; the presence of phosphatidylinositol enhances mechanosensitivity of the channel. May participate in the regulation of osmotic pressure changes within the cell.[UniProtKB:P9WJN5]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2oar ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2oar ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Mechanosensitive ion channels play a critical role in transducing physical stresses at the cell membrane into an electrochemical response. The MscL family of large-conductance mechanosensitive channels is widely distributed among prokaryotes and may participate in the regulation of osmotic pressure changes within the cell. In an effort to better understand the structural basis for the function of these channels, the structure of the MscL homolog from Mycobacterium tuberculosis was determined by x-ray crystallography to 3.5 angstroms resolution. This channel is organized as a homopentamer, with each subunit containing two transmembrane alpha helices and a third cytoplasmic alpha helix. From the extracellular side, a water-filled opening approximately 18 angstroms in diameter leads into a pore lined with hydrophilic residues which narrows at the cytoplasmic side to an occluded hydrophobic apex that may act as the channel gate. This structure may serve as a model for other mechanosensitive channels, as well as the broader class of pentameric ligand-gated ion channels exemplified by the nicotinic acetylcholine receptor.
 
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Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel.,Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC Science. 1998 Dec 18;282(5397):2220-6. PMID:9856938<ref>PMID:9856938</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2oar" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Ion channels 3D structures|Ion channels 3D structures]]
*[[Ion channels 3D structures|Ion channels 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mechanosensitive Channels]]
[[Category: Mechanosensitive Channels]]
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[[Category: Mycta]]
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[[Category: Mycobacterium tuberculosis H37Ra]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Chang, G]]
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[[Category: Chang G]]
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[[Category: Lee, A T]]
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[[Category: Lee AT]]
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[[Category: Rees, D C]]
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[[Category: Rees DC]]
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[[Category: Spencer, R H]]
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[[Category: Spencer RH]]
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[[Category: Steinbacher, S]]
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[[Category: Steinbacher S]]
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[[Category: Strop, P]]
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[[Category: Strop P]]
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[[Category: Membrane protein]]
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[[Category: Stretch activated ion channel mechanosensitive]]
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Current revision

Mechanosensitive Channel of Large Conductance (MscL)

PDB ID 2oar

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Proteopedia Page Contributors and Editors (what is this?)

OCA, Eric Martz, David S. Goodsell, Eran Hodis

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