Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals.
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.
Hite
Richard K
RK
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Li
Zongli
Z
Walz
Thomas
T
D000818:Animals; D020346:Aquaporins / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism*; D003461:Crystallography / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism*; D005136:Eye Proteins / Q000737:chemistry*; D007908:Lens, Crystalline / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry; D008055:Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D012756:Sheep; D014867:Water / Q000737:chemistry
D020346:Aquaporins; D005136:Eye Proteins; D008051:Lipid Bilayers; D008055:Lipids; D008565:Membrane Proteins; D011506:Proteins; C030328:aquaporin 0; D014867:Water; D004134:Dimyristoylphosphatidylcholine
EMBO Rep. 2007 Jan;8(1):51-5
17124511
Biochim Biophys Acta. 2004 Nov 3;1666(1-2):62-87
15519309
J Struct Biol. 2004 Jun;146(3):325-33
15099574
J Mol Biol. 1996 Jun 14;259(3):393-421
8676377
Nature. 2005 Dec 1;438(7068):633-8
16319884
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
15572765
Nature. 2004 May 13;429(6988):193-7
15141214
J Mol Biol. 1995 Aug 18;251(3):413-20
7544415
Biochim Biophys Acta. 2003 May 2;1612(1):1-40
12729927
Nature. 2000 Oct 5;407(6804):599-605
11034202
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21
9757107
Biochemistry. 1994 Feb 15;33(6):1606-15
8312280
J Mol Biol. 1999 Aug 27;291(4):899-911
10452895
Pflugers Arch. 2008 Jul;456(4):651-61
17932686
Biochim Biophys Acta. 2004 Nov 3;1666(1-2):2-18
15519305
Biochim Biophys Acta. 1976 Jul 20;441(1):38-47
782533
J Mol Biol. 2000 Aug 11;301(2):369-87
10926515
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
19461840
Biophys J. 2008 May 15;94(10):3996-4013
18234817
Rapid Commun Mass Spectrom. 2007;21(11):1721-8
17477452