دورية أكاديمية
Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes.
العنوان: | Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes. |
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المؤلفون: | Sonntag Y; Centre for Membrane Pumps in Cells and Disease - PUMPKIN, Danish National Research Foundation, DK-8000 Aarhus C, Denmark., Musgaard M, Olesen C, Schiøtt B, Møller JV, Nissen P, Thøgersen L |
المصدر: | Nature communications [Nat Commun] 2011; Vol. 2, pp. 304. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Print Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: [London] : Nature Pub. Group |
مواضيع طبية MeSH: | Sarcoplasmic Reticulum Calcium-Transporting ATPases/*chemistry, Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers/chemistry ; Models, Molecular ; Molecular Conformation ; Molecular Dynamics Simulation ; Phosphorylation ; Protein Structure, Secondary ; Protein Structure, Tertiary |
مستخلص: | The structural elucidation of membrane proteins continues to gather pace, but we know little about their molecular interactions with the lipid environment or how they interact with the surrounding bilayer. Here, with the aid of low-resolution X-ray crystallography, we present direct structural information on membrane interfaces as delineated by lipid phosphate groups surrounding the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) in its phosphorylated and dephosphorylated Ca(2+)-free forms. The protein-lipid interactions are further analysed using molecular dynamics simulations. We find that SERCA adapts to membranes of different hydrophobic thicknesses by inducing local deformations in the lipid bilayers and by undergoing small rearrangements of the amino-acid side chains and helix tilts. These mutually adaptive interactions allow smooth transitions through large conformational changes associated with the transport cycle of SERCA, a strategy that may be of general nature for many membrane proteins. |
References: | Biochemistry. 1993 Feb 16;32(6):1593-600. (PMID: 8431438) Curr Opin Struct Biol. 2009 Oct;19(5):560-5. (PMID: 19679462) J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674. (PMID: 19461840) Annu Rev Biophys. 2009;38:89-105. (PMID: 19416061) Biochim Biophys Acta. 1981 Mar 6;641(2):416-21. (PMID: 6111345) Biochim Biophys Acta. 2000 Nov 23;1508(1-2):86-111. (PMID: 11090820) Proteins. 2009 Sep;76(4):1007-19. (PMID: 19384996) J Mol Graph. 1996 Feb;14(1):33-8, 27-8. (PMID: 8744570) Eur J Biochem. 1983 Aug 1;134(2):205-14. (PMID: 6307686) J Comput Chem. 2004 Aug;25(11):1400-15. (PMID: 15185334) Biophys J. 2008 Aug;95(4):1590-9. (PMID: 18456821) Bioinformatics. 2006 Mar 1;22(5):623-5. (PMID: 16397007) Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2184-95. (PMID: 15572771) Nat Struct Biol. 2002 Sep;9(9):696-703. (PMID: 12172537) Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1355-63. (PMID: 15272157) Nature. 2009 May 21;459(7245):379-85. (PMID: 19458714) Curr Opin Struct Biol. 2008 Aug;18(4):406-11. (PMID: 18495472) FEBS Lett. 1982 Jul 19;144(1):145-8. (PMID: 6286354) Nature. 2003 Nov 6;426(6962):39-44. (PMID: 14603310) J Comput Chem. 2005 Dec;26(16):1781-802. (PMID: 16222654) J Phys Condens Matter. 2006 Jul 19;18(28):S1305-44. (PMID: 21690843) J Phys Chem B. 1998 Apr 30;102(18):3586-616. (PMID: 24889800) Biophys J. 1984 Aug;46(2):141-53. (PMID: 6478029) Biochemistry. 1981 Mar 31;20(7):1949-61. (PMID: 6452902) Biophys J. 2004 Jun;86(6):3620-33. (PMID: 15189859) Biochemistry. 1987 Jul 28;26(15):4803-10. (PMID: 3663628) J Biotechnol. 2006 Aug 5;124(4):704-16. (PMID: 16597471) Nature. 2009 Nov 26;462(7272):473-9. (PMID: 19940918) Proteins. 2008 Nov 15;73(3):765-83. (PMID: 18498103) Annu Rev Biophys Biomol Struct. 2007;36:107-30. (PMID: 17263662) Nature. 2005 Dec 1;438(7068):633-8. (PMID: 16319884) J Biol Chem. 1985 Jan 10;260(1):371-80. (PMID: 3155517) Biochim Biophys Acta. 2004 Nov 3;1666(1-2):205-26. (PMID: 15519316) Biochemistry. 1984 Dec 18;23(26):6901-11. (PMID: 6543323) Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32. (PMID: 15572765) Eur Biophys J. 2008 Apr;37(4):403-9. (PMID: 17960373) Acta Crystallogr D Biol Crystallogr. 2002 Nov;58(Pt 11):1948-54. (PMID: 12393927) J Biol Chem. 2010 Sep 10;285(37):28883-92. (PMID: 20551329) Nature. 2007 Dec 13;450(7172):1036-42. (PMID: 18075584) FEBS Lett. 2010 May 3;584(9):1713-20. (PMID: 20085759) Biophys J. 1998 Dec;75(6):2932-46. (PMID: 9826614) EMBO J. 2006 Jun 7;25(11):2305-14. (PMID: 16710301) Chem Phys Lipids. 1994 Sep 6;73(1-2):159-80. (PMID: 8001180) Nature. 2002 Aug 8;418(6898):605-11. (PMID: 12167852) Structure. 1999 Aug 15;7(8):909-17. (PMID: 10467143) Q Rev Biophys. 2010 Nov;43(4):501-66. (PMID: 20809990) Proteins. 2005 Dec 1;61(4):704-21. (PMID: 16231289) Biochim Biophys Acta. 2003 May 2;1612(1):1-40. (PMID: 12729927) |
المشرفين على المادة: | 0 (Lipid Bilayers) EC 3.6.3.8 (Sarcoplasmic Reticulum Calcium-Transporting ATPases) |
تواريخ الأحداث: | Date Created: 20110511 Date Completed: 20111104 Latest Revision: 20211020 |
رمز التحديث: | 20240628 |
DOI: | 10.1038/ncomms1307 |
PMID: | 21556058 |
قاعدة البيانات: | MEDLINE |
تدمد: | 2041-1723 |
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DOI: | 10.1038/ncomms1307 |