1sor
From Proteopedia
(New page: 200px<br /><applet load="1sor" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sor, resolution 3.00Å" /> '''Aquaporin-0 membrane...) |
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| - | [[Image:1sor.gif|left|200px]]<br /><applet load="1sor" size=" | + | [[Image:1sor.gif|left|200px]]<br /><applet load="1sor" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sor, resolution 3.00Å" /> | caption="1sor, resolution 3.00Å" /> | ||
'''Aquaporin-0 membrane junctions reveal the structure of a closed water pore'''<br /> | '''Aquaporin-0 membrane junctions reveal the structure of a closed water pore'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin | + | The lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin known to form membrane junctions in vivo. We show here that AQP0 from the lens core, containing some carboxy-terminally cleaved AQP0, forms double-layered crystals that recapitulate in vivo junctions. We present the structure of the AQP0 membrane junction as determined by electron crystallography. The junction is formed by three localized interactions between AQP0 molecules in adjoining membranes, mainly mediated by proline residues conserved in AQP0s from different species but not present in most other aquaporins. Whereas all previously determined aquaporin structures show the pore in an open conformation, the water pore is closed in AQP0 junctions. The water pathway in AQP0 also contains an additional pore constriction, not seen in other known aquaporin structures, which may be responsible for pore gating. |
==About this Structure== | ==About this Structure== | ||
| - | 1SOR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http:// | + | 1SOR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: water channel]] | [[Category: water channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:40 2008'' |
Revision as of 13:03, 21 February 2008
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Aquaporin-0 membrane junctions reveal the structure of a closed water pore
Overview
The lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin known to form membrane junctions in vivo. We show here that AQP0 from the lens core, containing some carboxy-terminally cleaved AQP0, forms double-layered crystals that recapitulate in vivo junctions. We present the structure of the AQP0 membrane junction as determined by electron crystallography. The junction is formed by three localized interactions between AQP0 molecules in adjoining membranes, mainly mediated by proline residues conserved in AQP0s from different species but not present in most other aquaporins. Whereas all previously determined aquaporin structures show the pore in an open conformation, the water pore is closed in AQP0 junctions. The water pathway in AQP0 also contains an additional pore constriction, not seen in other known aquaporin structures, which may be responsible for pore gating.
About this Structure
1SOR is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.
Reference
Aquaporin-0 membrane junctions reveal the structure of a closed water pore., Gonen T, Sliz P, Kistler J, Cheng Y, Walz T, Nature. 2004 May 13;429(6988):193-7. PMID:15141214
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