3M9I
Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) in E. coli polar lipids
Summary for 3M9I
| Entry DOI | 10.2210/pdb3m9i/pdb |
| Related | 1YMG 2B60 2C32 |
| Descriptor | Lens fiber major intrinsic protein, 1,2-Distearoyl-sn-glycerophosphoethanolamine (3 entities in total) |
| Functional Keywords | water channel, lens, lipid-protein interactions, membrane protein |
| Biological source | Ovis aries (domestic sheep,lambs,wild sheep) |
| Cellular location | Cell membrane ; Multi- pass membrane protein : Q6J8I9 |
| Total number of polymer chains | 1 |
| Total formula weight | 28750.90 |
| Authors | Hite, R.K.,Li, Z.,Walz, T. (deposition date: 2010-03-22, release date: 2010-05-12, Last modification date: 2023-09-06) |
| Primary citation | Hite, R.K.,Li, Z.,Walz, T. Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals. Embo J., 29:1652-1658, 2010 Cited by PubMed Abstract: 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. PubMed: 20389283DOI: 10.1038/emboj.2010.68 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (2.5 Å) |
Structure validation
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