کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2828722 | 1162752 | 2011 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A tool for the qualitative comparison of membrane-embedded and detergent-solubilized membrane protein structures in projection
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کلمات کلیدی
PDBGBFTMHProjection structurePsV - PSVtransmembrane α-helix - α-هلیکس فرابنفشTem - این استX-ray crystallography - بلورنگاری پرتو-ایکسTransporter - حمل کنندهTransmission electron microscopy - میکروسکوپ الکترونی عبوریProtein Data Bank - پروتئین بانک اطلاعاتیMembrane protein - پروتئین غشائیTwo-dimensional crystal - کریستال دو بعدیElectron crystallography - کریستالوگرافی الکترون
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The calculation of projection structures (PSs) from Protein Data Bank (PDB)-coordinate files of membrane proteins is not well-established. Reports on such attempts exist but are rare. In addition, the different procedures are barely described and thus difficult if not impossible to reproduce. Here we present a simple, fast and well-documented method for the calculation and visualization of PSs from PDB-coordinate files of membrane proteins: the projection structure visualization (PSV)-method. The PSV-method was successfully validated using the PS of aquaporin-1 (AQP1) from 2D crystals and cryo-transmission electron microscopy, and the PDB-coordinate file of AQP1 determined from 3D crystals and X-ray crystallography. Besides AQP1, which is a relatively rigid protein, we also studied a flexible membrane transport protein, i.e. the l-arginine/agmatine antiporter AdiC. Comparison of PSs calculated from the existing PDB-coordinate files of substrate-free and l-arginine-bound AdiC indicated that conformational changes are detected in projection. Importantly, structural differences were found between the PSV-method calculated PSs of the detergent-solubilized AdiC proteins and the PS from cryo-TEM of membrane-embedded AdiC. These differences are particularly exciting since they may reflect a different conformation of AdiC induced by the lateral pressure in the lipid bilayer.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 173, Issue 2, February 2011, Pages 375-381
Journal: Journal of Structural Biology - Volume 173, Issue 2, February 2011, Pages 375-381
نویسندگان
Jean-Marc Jeckelmann, Manuel Palacin, Dimitrios Fotiadis,