دورية أكاديمية
أعرض في EDS

Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes.

التفاصيل البيبلوغرافية
العنوان: Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes.
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.
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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
الوصف
تدمد:2041-1723
DOI:10.1038/ncomms1307