3m9i

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Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) in E. coli polar lipids

Structural highlights

3m9i is a 1 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron crystallography, Resolution 2.5Å
Ligands:3PE
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MIP_SHEEP Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We have previously described the interactions of aquaporin-0 (AQP0) with dimyristoyl phosphatidylcholine (DMPC) lipids. We have now determined the 2.5 A structure of AQP0 in two-dimensional (2D) crystals formed with Escherichia coli polar lipids (EPLs), which differ from DMPC both in headgroups and acyl chains. Comparison of the two structures shows that AQP0 does not adapt to the different length of the acyl chains in EPLs and that the distance between the phosphodiester groups in the two leaflets of the DMPC and EPL bilayers is almost identical. The EPL headgroups interact differently with AQP0 than do those of DMPC, but the acyl chains in the EPL and DMPC bilayers occupy similar positions. The interactions of annular lipids with membrane proteins seem to be driven by the propensity of the acyl chains to fill gaps in the protein surface. Interactions of the lipid headgroups may be responsible for the specific interactions found in tightly bound lipids but seem to have a negligible effect on interactions of generic annular lipids with membrane proteins.

Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals.,Hite RK, Li Z, Walz T EMBO J. 2010 May 19;29(10):1652-8. Epub 2010 Apr 13. PMID:20389283[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. ↑ Gonen T, Sliz P, Kistler J, Cheng Y, Walz T. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature. 2004 May 13;429(6988):193-7. PMID:15141214 doi:10.1038/nature02503
  2. ↑ Gonen T, Cheng Y, Kistler J, Walz T. Aquaporin-0 membrane junctions form upon proteolytic cleavage. J Mol Biol. 2004 Sep 24;342(4):1337-45. PMID:15351655 doi:http://dx.doi.org/10.1016/j.jmb.2004.07.076
  3. ↑ Hite RK, Li Z, Walz T. Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals. EMBO J. 2010 May 19;29(10):1652-8. Epub 2010 Apr 13. PMID:20389283 doi:10.1038/emboj.2010.68
  4. ↑ Hite RK, Li Z, Walz T. Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals. EMBO J. 2010 May 19;29(10):1652-8. Epub 2010 Apr 13. PMID:20389283 doi:10.1038/emboj.2010.68

Contents


PDB ID 3m9i

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