2oar
From Proteopedia
(New page: 200px<br /><applet load="2oar" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oar, resolution 3.50Å" /> '''Mechanosensitive Cha...) |
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| - | [[Image:2oar.gif|left|200px]]<br /><applet load="2oar" size=" | + | [[Image:2oar.gif|left|200px]]<br /><applet load="2oar" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2oar, resolution 3.50Å" /> | caption="2oar, resolution 3.50Å" /> | ||
'''Mechanosensitive Channel of Large Conductance (MscL)'''<br /> | '''Mechanosensitive Channel of Large Conductance (MscL)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mechanosensitive ion channels play a critical role in transducing physical | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2OAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with AU as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 2OAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=AU:'>AU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1MSL. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OAR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chang, G.]] | [[Category: Chang, G.]] | ||
| - | [[Category: Lee, A | + | [[Category: Lee, A T.]] |
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
| - | [[Category: Spencer, R | + | [[Category: Spencer, R H.]] |
[[Category: Steinbacher, S.]] | [[Category: Steinbacher, S.]] | ||
[[Category: Strop, P.]] | [[Category: Strop, P.]] | ||
| Line 22: | Line 22: | ||
[[Category: stretch activated ion channel mechanosensitive]] | [[Category: stretch activated ion channel mechanosensitive]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:20 2008'' |
Revision as of 16:16, 21 February 2008
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Mechanosensitive Channel of Large Conductance (MscL)
Overview
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.
About this Structure
2OAR is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. This structure supersedes the now removed PDB entry 1MSL. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 18:16:20 2008
